Full text data of BMP2K
BMP2K
(BIKE)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
BMP-2-inducible protein kinase; BIKe; 2.7.11.1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
BMP-2-inducible protein kinase; BIKe; 2.7.11.1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NSY1
ID BMP2K_HUMAN Reviewed; 1161 AA.
AC Q9NSY1; O94791; Q8IYF2; Q8N2G7; Q8NHG9; Q9NTG8;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-AUG-2003, sequence version 2.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=BMP-2-inducible protein kinase;
DE Short=BIKe;
DE EC=2.7.11.1;
GN Name=BMP2K; Synonyms=BIKE; ORFNames=HRIHFB2017;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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 MRNA] (ISOFORM 2), AND VARIANT
RP 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-834 AND SER-1076, AND
RP MASS SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-1107, AND
RP MASS SPECTROMETRY.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1032, AND
RP MASS SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029; SER-1107 AND
RP SER-1111, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
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.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., 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 -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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 Note=No experimental confirmation available;
CC -!- PTM: Autophosphorylated (By similarity).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC protein kinase family.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK075278; BAC11515.1; -; mRNA.
DR EMBL; AL137275; CAB70673.1; -; mRNA.
DR EMBL; AL137661; CAB70863.1; -; mRNA.
DR EMBL; BC036021; AAH36021.1; -; mRNA.
DR EMBL; AF527532; AAM88867.1; -; mRNA.
DR EMBL; AB015331; BAA34790.1; -; mRNA.
DR PIR; T46347; T46347.
DR PIR; T46364; T46364.
DR RefSeq; NP_060063.2; NM_017593.3.
DR RefSeq; NP_942595.1; NM_198892.1.
DR UniGene; Hs.146551; -.
DR ProteinModelPortal; Q9NSY1; -.
DR SMR; Q9NSY1; 46-378.
DR IntAct; Q9NSY1; 3.
DR STRING; 9606.ENSP00000334836; -.
DR BindingDB; Q9NSY1; -.
DR ChEMBL; CHEMBL4522; -.
DR GuidetoPHARMACOLOGY; 1941; -.
DR PhosphoSite; Q9NSY1; -.
DR DMDM; 34222653; -.
DR PaxDb; Q9NSY1; -.
DR PRIDE; Q9NSY1; -.
DR DNASU; 55589; -.
DR Ensembl; ENST00000335016; ENSP00000334836; ENSG00000138756.
DR Ensembl; ENST00000502871; ENSP00000421768; ENSG00000138756.
DR GeneID; 55589; -.
DR KEGG; hsa:55589; -.
DR UCSC; uc003hlk.3; human.
DR CTD; 55589; -.
DR GeneCards; GC04P079697; -.
DR HGNC; HGNC:18041; BMP2K.
DR HPA; HPA026436; -.
DR HPA; HPA026451; -.
DR HPA; HPA026501; -.
DR neXtProt; NX_Q9NSY1; -.
DR PharmGKB; PA134992822; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000095243; -.
DR HOVERGEN; HBG050703; -.
DR InParanoid; Q9NSY1; -.
DR KO; K08854; -.
DR OMA; DAYMQQY; -.
DR OrthoDB; EOG7PP566; -.
DR SignaLink; Q9NSY1; -.
DR ChiTaRS; BMP2K; human.
DR GeneWiki; BMP2K; -.
DR GenomeRNAi; 55589; -.
DR NextBio; 60112; -.
DR PRO; PR:Q9NSY1; -.
DR ArrayExpress; Q9NSY1; -.
DR Bgee; Q9NSY1; -.
DR CleanEx; HS_BMP2K; -.
DR Genevestigator; Q9NSY1; -.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019208; F:phosphatase regulator activity; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030500; P:regulation of bone mineralization; IEA:Ensembl.
DR InterPro; IPR028182; BMP2K_C.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF15282; BMP2K_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
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; Complete proteome; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1 1161 BMP-2-inducible protein kinase.
FT /FTId=PRO_0000085663.
FT DOMAIN 51 316 Protein kinase.
FT NP_BIND 57 65 ATP (By similarity).
FT COMPBIAS 12 40 Gly-rich.
FT COMPBIAS 425 559 Gln/His-rich.
FT ACT_SITE 180 180 Proton acceptor (By similarity).
FT BINDING 79 79 ATP (By similarity).
FT MOD_RES 14 14 Phosphoserine.
FT MOD_RES 834 834 Phosphothreonine.
FT MOD_RES 928 928 Phosphoserine (By similarity).
FT MOD_RES 1029 1029 Phosphoserine.
FT MOD_RES 1031 1031 Phosphoserine (By similarity).
FT MOD_RES 1032 1032 Phosphoserine.
FT MOD_RES 1076 1076 Phosphoserine.
FT MOD_RES 1107 1107 Phosphoserine.
FT MOD_RES 1111 1111 Phosphoserine.
FT VAR_SEQ 330 340 NSSIPSALPEP -> KCCKQLLRHGALLTEILLFLQLFLNR
FT (in isoform 3).
FT /FTId=VSP_008093.
FT VAR_SEQ 651 662 NRLEERASSDKN -> SKGHLKAYFASQ (in isoform
FT 2 and isoform 3).
FT /FTId=VSP_008091.
FT VAR_SEQ 663 1161 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_008092.
FT VARIANT 68 68 V -> M (in a lung squamous cell carcinoma
FT sample; somatic mutation).
FT /FTId=VAR_040388.
FT VARIANT 212 212 D -> V (in dbSNP:rs56143363).
FT /FTId=VAR_040389.
FT VARIANT 288 288 R -> H (in dbSNP:rs55782848).
FT /FTId=VAR_040390.
FT VARIANT 405 405 G -> S (in dbSNP:rs2288255).
FT /FTId=VAR_051618.
FT VARIANT 486 486 Q -> H (in dbSNP:rs2114202).
FT /FTId=VAR_059765.
FT VARIANT 1002 1002 T -> S (in dbSNP:rs12507099).
FT /FTId=VAR_051619.
FT CONFLICT 342 342 T -> A (in Ref. 3; AAH36021).
FT CONFLICT 471 486 Missing (in Ref. 2; CAB70863).
FT CONFLICT 478 478 Q -> R (in Ref. 3; AAH36021).
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
//
ID BMP2K_HUMAN Reviewed; 1161 AA.
AC Q9NSY1; O94791; Q8IYF2; Q8N2G7; Q8NHG9; Q9NTG8;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-AUG-2003, sequence version 2.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=BMP-2-inducible protein kinase;
DE Short=BIKe;
DE EC=2.7.11.1;
GN Name=BMP2K; Synonyms=BIKE; ORFNames=HRIHFB2017;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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 MRNA] (ISOFORM 2), AND VARIANT
RP 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-834 AND SER-1076, AND
RP MASS SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-1107, AND
RP MASS SPECTROMETRY.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1032, AND
RP MASS SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029; SER-1107 AND
RP SER-1111, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
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.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., 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 -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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 Note=No experimental confirmation available;
CC -!- PTM: Autophosphorylated (By similarity).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC protein kinase family.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK075278; BAC11515.1; -; mRNA.
DR EMBL; AL137275; CAB70673.1; -; mRNA.
DR EMBL; AL137661; CAB70863.1; -; mRNA.
DR EMBL; BC036021; AAH36021.1; -; mRNA.
DR EMBL; AF527532; AAM88867.1; -; mRNA.
DR EMBL; AB015331; BAA34790.1; -; mRNA.
DR PIR; T46347; T46347.
DR PIR; T46364; T46364.
DR RefSeq; NP_060063.2; NM_017593.3.
DR RefSeq; NP_942595.1; NM_198892.1.
DR UniGene; Hs.146551; -.
DR ProteinModelPortal; Q9NSY1; -.
DR SMR; Q9NSY1; 46-378.
DR IntAct; Q9NSY1; 3.
DR STRING; 9606.ENSP00000334836; -.
DR BindingDB; Q9NSY1; -.
DR ChEMBL; CHEMBL4522; -.
DR GuidetoPHARMACOLOGY; 1941; -.
DR PhosphoSite; Q9NSY1; -.
DR DMDM; 34222653; -.
DR PaxDb; Q9NSY1; -.
DR PRIDE; Q9NSY1; -.
DR DNASU; 55589; -.
DR Ensembl; ENST00000335016; ENSP00000334836; ENSG00000138756.
DR Ensembl; ENST00000502871; ENSP00000421768; ENSG00000138756.
DR GeneID; 55589; -.
DR KEGG; hsa:55589; -.
DR UCSC; uc003hlk.3; human.
DR CTD; 55589; -.
DR GeneCards; GC04P079697; -.
DR HGNC; HGNC:18041; BMP2K.
DR HPA; HPA026436; -.
DR HPA; HPA026451; -.
DR HPA; HPA026501; -.
DR neXtProt; NX_Q9NSY1; -.
DR PharmGKB; PA134992822; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000095243; -.
DR HOVERGEN; HBG050703; -.
DR InParanoid; Q9NSY1; -.
DR KO; K08854; -.
DR OMA; DAYMQQY; -.
DR OrthoDB; EOG7PP566; -.
DR SignaLink; Q9NSY1; -.
DR ChiTaRS; BMP2K; human.
DR GeneWiki; BMP2K; -.
DR GenomeRNAi; 55589; -.
DR NextBio; 60112; -.
DR PRO; PR:Q9NSY1; -.
DR ArrayExpress; Q9NSY1; -.
DR Bgee; Q9NSY1; -.
DR CleanEx; HS_BMP2K; -.
DR Genevestigator; Q9NSY1; -.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019208; F:phosphatase regulator activity; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030500; P:regulation of bone mineralization; IEA:Ensembl.
DR InterPro; IPR028182; BMP2K_C.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF15282; BMP2K_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
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; Complete proteome; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1 1161 BMP-2-inducible protein kinase.
FT /FTId=PRO_0000085663.
FT DOMAIN 51 316 Protein kinase.
FT NP_BIND 57 65 ATP (By similarity).
FT COMPBIAS 12 40 Gly-rich.
FT COMPBIAS 425 559 Gln/His-rich.
FT ACT_SITE 180 180 Proton acceptor (By similarity).
FT BINDING 79 79 ATP (By similarity).
FT MOD_RES 14 14 Phosphoserine.
FT MOD_RES 834 834 Phosphothreonine.
FT MOD_RES 928 928 Phosphoserine (By similarity).
FT MOD_RES 1029 1029 Phosphoserine.
FT MOD_RES 1031 1031 Phosphoserine (By similarity).
FT MOD_RES 1032 1032 Phosphoserine.
FT MOD_RES 1076 1076 Phosphoserine.
FT MOD_RES 1107 1107 Phosphoserine.
FT MOD_RES 1111 1111 Phosphoserine.
FT VAR_SEQ 330 340 NSSIPSALPEP -> KCCKQLLRHGALLTEILLFLQLFLNR
FT (in isoform 3).
FT /FTId=VSP_008093.
FT VAR_SEQ 651 662 NRLEERASSDKN -> SKGHLKAYFASQ (in isoform
FT 2 and isoform 3).
FT /FTId=VSP_008091.
FT VAR_SEQ 663 1161 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_008092.
FT VARIANT 68 68 V -> M (in a lung squamous cell carcinoma
FT sample; somatic mutation).
FT /FTId=VAR_040388.
FT VARIANT 212 212 D -> V (in dbSNP:rs56143363).
FT /FTId=VAR_040389.
FT VARIANT 288 288 R -> H (in dbSNP:rs55782848).
FT /FTId=VAR_040390.
FT VARIANT 405 405 G -> S (in dbSNP:rs2288255).
FT /FTId=VAR_051618.
FT VARIANT 486 486 Q -> H (in dbSNP:rs2114202).
FT /FTId=VAR_059765.
FT VARIANT 1002 1002 T -> S (in dbSNP:rs12507099).
FT /FTId=VAR_051619.
FT CONFLICT 342 342 T -> A (in Ref. 3; AAH36021).
FT CONFLICT 471 486 Missing (in Ref. 2; CAB70863).
FT CONFLICT 478 478 Q -> R (in Ref. 3; AAH36021).
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
//