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Q9NSY1

- BMP2K_HUMAN

UniProt

Q9NSY1 - BMP2K_HUMAN

Protein

BMP-2-inducible protein kinase

Gene

BMP2K

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (22 Aug 2003)
      Previous versions | rss
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    Functioni

    May be involved in osteoblast differentiation.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei79 – 791ATPPROSITE-ProRule annotation
    Active sitei180 – 1801Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi57 – 659ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphatase regulator activity Source: Ensembl
    3. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. regulation of bone mineralization Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ9NSY1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    BMP-2-inducible protein kinase (EC:2.7.11.1)
    Short name:
    BIKe
    Gene namesi
    Name:BMP2K
    Synonyms:BIKE
    ORF Names:HRIHFB2017
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:18041. BMP2K.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134992822.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11611161BMP-2-inducible protein kinasePRO_0000085663Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141Phosphoserine1 Publication
    Modified residuei834 – 8341Phosphothreonine1 Publication
    Modified residuei928 – 9281PhosphoserineBy similarity
    Modified residuei1029 – 10291Phosphoserine2 Publications
    Modified residuei1031 – 10311PhosphoserineBy similarity
    Modified residuei1032 – 10321Phosphoserine1 Publication
    Modified residuei1076 – 10761Phosphoserine1 Publication
    Modified residuei1107 – 11071Phosphoserine3 Publications
    Modified residuei1111 – 11111Phosphoserine1 Publication

    Post-translational modificationi

    Autophosphorylated.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NSY1.
    PaxDbiQ9NSY1.
    PRIDEiQ9NSY1.

    PTM databases

    PhosphoSiteiQ9NSY1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NSY1.
    BgeeiQ9NSY1.
    CleanExiHS_BMP2K.
    GenevestigatoriQ9NSY1.

    Organism-specific databases

    HPAiHPA026436.
    HPA026451.
    HPA026501.

    Interactioni

    Protein-protein interaction databases

    BioGridi120735. 7 interactions.
    IntActiQ9NSY1. 3 interactions.
    STRINGi9606.ENSP00000334836.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NSY1.
    SMRiQ9NSY1. Positions 46-378.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini51 – 316266Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi12 – 4029Gly-richAdd
    BLAST
    Compositional biasi425 – 559135Gln/His-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000095243.
    HOVERGENiHBG050703.
    InParanoidiQ9NSY1.
    KOiK08854.
    OMAiVPFISHP.
    OrthoDBiEOG7PP566.
    PhylomeDBiQ9NSY1.
    TreeFamiTF335936.

    Family and domain databases

    InterProiIPR026105. BMP-2-ind_kinase.
    IPR028182. BMP2K_C.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR22967:SF10. PTHR22967:SF10. 1 hit.
    PfamiPF15282. BMP2K_C. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NSY1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKKFSRMPKS EGGSGGGAAG GGAGGAGAGA GCGSGGSSVG VRVFAVGRHQ     50
    VTLEESLAEG GFSTVFLVRT HGGIRCALKR MYVNNMPDLN VCKREITIMK 100
    ELSGHKNIVG YLDCAVNSIS DNVWEVLILM EYCRAGQVVN QMNKKLQTGF 150
    TEPEVLQIFC DTCEAVARLH QCKTPIIHRD LKVENILLND GGNYVLCDFG 200
    SATNKFLNPQ KDGVNVVEEE IKKYTTLSYR APEMINLYGG KPITTKADIW 250
    ALGCLLYKLC FFTLPFGESQ VAICDGNFTI PDNSRYSRNI HCLIRFMLEP 300
    DPEHRPDIFQ VSYFAFKFAK KDCPVSNINN SSIPSALPEP MTASEAAARK 350
    SQIKARITDT IGPTETSIAP RQRPKANSAT TATPSVLTIQ SSATPVKVLA 400
    PGEFGNHRPK GALRPGNGPE ILLGQGPPQQ PPQQHRVLQQ LQQGDWRLQQ 450
    LHLQHRHPHQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQHHHH HHHHLLQDAY 500
    MQQYQHATQQ QQMLQQQFLM HSVYQPQPSA SQYPTMMPQY QQAFFQQQML 550
    AQHQPSQQQA SPEYLTSPQE FSPALVSYTS SLPAQVGTIM DSSYSANRSV 600
    ADKEAIANFT NQKNISNPPD MSGWNPFGED NFSKLTEEEL LDREFDLLRS 650
    NRLEERASSD KNVDSLSAPH NHPPEDPFGS VPFISHSGSP EKKAEHSSIN 700
    QENGTANPIK NGKTSPASKD QRTGKKTSVQ GQVQKGNDES ESDFESDPPS 750
    PKSSEEEEQD DEEVLQGEQG DFNDDDTEPE NLGHRPLLMD SEDEEEEEKH 800
    SSDSDYEQAK AKYSDMSSVY RDRSGSGPTQ DLNTILLTSA QLSSDVAVET 850
    PKQEFDVFGA VPFFAVRAQQ PQQEKNEKNL PQHRFPAAGL EQEEFDVFTK 900
    APFSKKVNVQ ECHAVGPEAH TIPGYPKSVD VFGSTPFQPF LTSTSKSESN 950
    EDLFGLVPFD EITGSQQQKV KQRSLQKLSS RQRRTKQDMS KSNGKRHHGT 1000
    PTSTKKTLKP TYRTPERARR HKKVGRRDSQ SSNEFLTISD SKENISVALT 1050
    DGKDRGNVLQ PEESLLDPFG AKPFHSPDLS WHPPHQGLSD IRADHNTVLP 1100
    GRPRQNSLHG SFHSADVLKM DDFGAVPFTE LVVQSITPHQ SQQSQPVELD 1150
    PFGAAPFPSK Q 1161
    Length:1,161
    Mass (Da):129,172
    Last modified:August 22, 2003 - v2
    Checksum:i5C38A86E95935EC2
    GO
    Isoform 2 (identifier: Q9NSY1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         651-662: NRLEERASSDKN → SKGHLKAYFASQ
         663-1161: Missing.

    Show »
    Length:662
    Mass (Da):73,838
    Checksum:iED443E4DC0696FF3
    GO
    Isoform 3 (identifier: Q9NSY1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         330-340: NSSIPSALPEP → KCCKQLLRHGALLTEILLFLQLFLNR
         651-662: NRLEERASSDKN → SKGHLKAYFASQ
         663-1161: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:677
    Mass (Da):75,812
    Checksum:iFF17E464DB5F952C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti342 – 3421T → A in AAH36021. (PubMed:15489334)Curated
    Sequence conflicti471 – 48616Missing in CAB70863. (PubMed:17974005)CuratedAdd
    BLAST
    Sequence conflicti478 – 4781Q → R in AAH36021. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti68 – 681V → M in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
    VAR_040388
    Natural varianti212 – 2121D → V.1 Publication
    Corresponds to variant rs56143363 [ dbSNP | Ensembl ].
    VAR_040389
    Natural varianti288 – 2881R → H.1 Publication
    Corresponds to variant rs55782848 [ dbSNP | Ensembl ].
    VAR_040390
    Natural varianti405 – 4051G → S.1 Publication
    Corresponds to variant rs2288255 [ dbSNP | Ensembl ].
    VAR_051618
    Natural varianti486 – 4861Q → H.
    Corresponds to variant rs2114202 [ dbSNP | Ensembl ].
    VAR_059765
    Natural varianti1002 – 10021T → S.
    Corresponds to variant rs12507099 [ dbSNP | Ensembl ].
    VAR_051619

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei330 – 34011NSSIPSALPEP → KCCKQLLRHGALLTEILLFL QLFLNR in isoform 3. 1 PublicationVSP_008093Add
    BLAST
    Alternative sequencei651 – 66212NRLEE…SSDKN → SKGHLKAYFASQ in isoform 2 and isoform 3. 4 PublicationsVSP_008091Add
    BLAST
    Alternative sequencei663 – 1161499Missing in isoform 2 and isoform 3. 4 PublicationsVSP_008092Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK075278 mRNA. Translation: BAC11515.1.
    AK292147 mRNA. Translation: BAF84836.1.
    AL137275 mRNA. Translation: CAB70673.1.
    AL137661 mRNA. Translation: CAB70863.1.
    AC098818 Genomic DNA. Translation: AAY40926.1.
    BC036021 mRNA. Translation: AAH36021.1.
    AF527532 mRNA. Translation: AAM88867.1.
    AB015331 mRNA. Translation: BAA34790.1.
    CCDSiCCDS34019.1. [Q9NSY1-2]
    CCDS47083.1. [Q9NSY1-1]
    PIRiT46347.
    T46364.
    RefSeqiNP_060063.2. NM_017593.3. [Q9NSY1-2]
    NP_942595.1. NM_198892.1. [Q9NSY1-1]
    UniGeneiHs.146551.

    Genome annotation databases

    EnsembliENST00000335016; ENSP00000334836; ENSG00000138756. [Q9NSY1-1]
    ENST00000502871; ENSP00000421768; ENSG00000138756. [Q9NSY1-2]
    GeneIDi55589.
    KEGGihsa:55589.
    UCSCiuc003hlk.3. human. [Q9NSY1-1]

    Polymorphism databases

    DMDMi34222653.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK075278 mRNA. Translation: BAC11515.1 .
    AK292147 mRNA. Translation: BAF84836.1 .
    AL137275 mRNA. Translation: CAB70673.1 .
    AL137661 mRNA. Translation: CAB70863.1 .
    AC098818 Genomic DNA. Translation: AAY40926.1 .
    BC036021 mRNA. Translation: AAH36021.1 .
    AF527532 mRNA. Translation: AAM88867.1 .
    AB015331 mRNA. Translation: BAA34790.1 .
    CCDSi CCDS34019.1. [Q9NSY1-2 ]
    CCDS47083.1. [Q9NSY1-1 ]
    PIRi T46347.
    T46364.
    RefSeqi NP_060063.2. NM_017593.3. [Q9NSY1-2 ]
    NP_942595.1. NM_198892.1. [Q9NSY1-1 ]
    UniGenei Hs.146551.

    3D structure databases

    ProteinModelPortali Q9NSY1.
    SMRi Q9NSY1. Positions 46-378.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120735. 7 interactions.
    IntActi Q9NSY1. 3 interactions.
    STRINGi 9606.ENSP00000334836.

    Chemistry

    BindingDBi Q9NSY1.
    ChEMBLi CHEMBL4522.
    GuidetoPHARMACOLOGYi 1941.

    PTM databases

    PhosphoSitei Q9NSY1.

    Polymorphism databases

    DMDMi 34222653.

    Proteomic databases

    MaxQBi Q9NSY1.
    PaxDbi Q9NSY1.
    PRIDEi Q9NSY1.

    Protocols and materials databases

    DNASUi 55589.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335016 ; ENSP00000334836 ; ENSG00000138756 . [Q9NSY1-1 ]
    ENST00000502871 ; ENSP00000421768 ; ENSG00000138756 . [Q9NSY1-2 ]
    GeneIDi 55589.
    KEGGi hsa:55589.
    UCSCi uc003hlk.3. human. [Q9NSY1-1 ]

    Organism-specific databases

    CTDi 55589.
    GeneCardsi GC04P079697.
    HGNCi HGNC:18041. BMP2K.
    HPAi HPA026436.
    HPA026451.
    HPA026501.
    neXtProti NX_Q9NSY1.
    PharmGKBi PA134992822.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000095243.
    HOVERGENi HBG050703.
    InParanoidi Q9NSY1.
    KOi K08854.
    OMAi VPFISHP.
    OrthoDBi EOG7PP566.
    PhylomeDBi Q9NSY1.
    TreeFami TF335936.

    Enzyme and pathway databases

    SignaLinki Q9NSY1.

    Miscellaneous databases

    ChiTaRSi BMP2K. human.
    GeneWikii BMP2K.
    GenomeRNAii 55589.
    NextBioi 60112.
    PROi Q9NSY1.

    Gene expression databases

    ArrayExpressi Q9NSY1.
    Bgeei Q9NSY1.
    CleanExi HS_BMP2K.
    Genevestigatori Q9NSY1.

    Family and domain databases

    InterProi IPR026105. BMP-2-ind_kinase.
    IPR028182. BMP2K_C.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR22967:SF10. PTHR22967:SF10. 1 hit.
    Pfami PF15282. BMP2K_C. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Synovium and Thyroid.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Testis.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT SER-405.
      Tissue: Testis.
    5. Guo J.H., Yu L.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 537-1161 (ISOFORM 2).
      Tissue: Ovary.
    6. "Selection system for genes encoding nuclear-targeted proteins."
      Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
      Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 946-1161 (ISOFORM 1), SUBCELLULAR LOCATION.
      Tissue: Brain.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-834 AND SER-1076, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-1107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1032, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029; SER-1107 AND SER-1111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-68; VAL-212 AND HIS-288.

    Entry informationi

    Entry nameiBMP2K_HUMAN
    AccessioniPrimary (citable) accession number: Q9NSY1
    Secondary accession number(s): O94791
    , Q4W5H2, Q8IYF2, Q8N2G7, Q8NHG9, Q9NTG8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 22, 2003
    Last sequence update: August 22, 2003
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3