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P36898

- BMR1B_MOUSE

UniProt

P36898 - BMR1B_MOUSE

Protein

Bone morphogenetic protein receptor type-1B

Gene

Bmpr1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5.

    Catalytic activityi

    ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.

    Cofactori

    Magnesium or manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei231 – 2311ATPPROSITE-ProRule annotation
    Active sitei332 – 3321Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi210 – 2189ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. receptor signaling protein serine/threonine kinase activity Source: InterPro
    5. transforming growth factor beta-activated receptor activity Source: MGI
    6. transforming growth factor beta receptor activity, type I Source: MGI

    GO - Biological processi

    1. BMP signaling pathway Source: MGI
    2. camera-type eye development Source: MGI
    3. cartilage condensation Source: MGI
    4. cell differentiation Source: MGI
    5. chondrocyte differentiation Source: MGI
    6. dorsal/ventral pattern formation Source: MGI
    7. estrogen biosynthetic process Source: UniProtKB
    8. eye development Source: MGI
    9. inflammatory response Source: UniProtKB
    10. limb morphogenesis Source: Ensembl
    11. ovarian cumulus expansion Source: UniProtKB
    12. ovulation cycle Source: UniProtKB
    13. positive regulation of bone mineralization Source: Ensembl
    14. positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
    15. positive regulation of osteoblast differentiation Source: Ensembl
    16. retina development in camera-type eye Source: MGI
    17. retinal ganglion cell axon guidance Source: MGI
    18. transforming growth factor beta receptor signaling pathway Source: MGI
    19. transmembrane receptor protein serine/threonine kinase signaling pathway Source: MGI

    Keywords - Molecular functioni

    Kinase, Receptor, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Chondrogenesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 3474.
    ReactomeiREACT_220505. Signaling by BMP.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bone morphogenetic protein receptor type-1B (EC:2.7.11.30)
    Short name:
    BMP type-1B receptor
    Short name:
    BMPR-1B
    Alternative name(s):
    Activin receptor-like kinase 6
    Short name:
    ALK-6
    Serine/threonine-protein kinase receptor R6
    Short name:
    SKR6
    CD_antigen: CDw293
    Gene namesi
    Name:Bmpr1b
    Synonyms:Acvrlk6
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:107191. Bmpr1b.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1313Sequence AnalysisAdd
    BLAST
    Chaini14 – 502489Bone morphogenetic protein receptor type-1BPRO_0000024413Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi32 ↔ 531 Publication
    Disulfide bondi34 ↔ 381 Publication
    Disulfide bondi47 ↔ 711 Publication
    Disulfide bondi81 ↔ 951 Publication
    Disulfide bondi96 ↔ 1021 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP36898.
    PRIDEiP36898.

    PTM databases

    PhosphoSiteiP36898.

    Expressioni

    Gene expression databases

    ArrayExpressiP36898.
    BgeeiP36898.
    CleanExiMM_BMPR1B.
    GenevestigatoriP36898.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Smad6O351822EBI-7107883,EBI-4321242

    Protein-protein interaction databases

    DIPiDIP-252N.
    IntActiP36898. 1 interaction.
    MINTiMINT-124245.

    Structurei

    Secondary structure

    1
    502
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 334
    Beta strandi35 – 373
    Beta strandi46 – 5914
    Beta strandi64 – 729
    Helixi77 – 804
    Beta strandi91 – 966
    Helixi102 – 1054

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EVSX-ray2.10C14-126[»]
    ProteinModelPortaliP36898.
    SMRiP36898. Positions 29-113, 174-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36898.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini14 – 126113ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini149 – 502354CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei127 – 14822HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini174 – 20330GSPROSITE-ProRule annotationAdd
    BLAST
    Domaini204 – 494291Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 GS domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00730000110337.
    HOGENOMiHOG000230587.
    HOVERGENiHBG054502.
    InParanoidiP36898.
    KOiK13578.
    OMAiLRCKCHH.
    OrthoDBiEOG7Q8CN3.
    PhylomeDBiP36898.
    TreeFamiTF314724.

    Family and domain databases

    InterProiIPR000472. Activin_rcpt.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    IPR003605. TGF_beta_rcpt_GS.
    IPR000333. TGFB_receptor.
    [Graphical view]
    PANTHERiPTHR23255. PTHR23255. 1 hit.
    PfamiPF01064. Activin_recp. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF08515. TGF_beta_GS. 1 hit.
    [Graphical view]
    SMARTiSM00467. GS. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51256. GS. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P36898-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLRSSGKLN VGTKKEDGES TAPTPRPKIL RCKCHHHCPE DSVNNICSTD    50
    GYCFTMIEED DSGMPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN 100
    ECNKDLHPTL PPLKDRDFVD GPIHHKALLI SVTVCSLLLV LIILFCYFRY 150
    KRQEARPRYS IGLEQDETYI PPGESLRDLI EQSQSSGSGS GLPLLVQRTI 200
    AKQIQMVKQI GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS WFRETEIYQT 250
    VLMRHENILG FIAADIKGTG SWTQLYLITD YHENGSLYDY LKSTTLDAKS 300
    MLKLAYSSVS GLCHLHTEIF STQGKPAIAH RDLKSKNILV KKNGTCCIAD 350
    LGLAVKFISD TNEVDIPPNT RVGTKRYMPP EVLDESLNRN HFQSYIMADM 400
    YSFGLILWEI ARRCVSGGIV EEYQLPYHDL VPSDPSYEDM REIVCMKKLR 450
    PSFPNRWSSD ECLRQMGKLM TECWAQNPAS RLTALRVKKT LAKMSESQDI 500
    KL 502
    Length:502
    Mass (Da):56,944
    Last modified:June 1, 1994 - v1
    Checksum:iAB29681F3FF5A361
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z23143 mRNA. Translation: CAA80674.1.
    AK086130 mRNA. Translation: BAC39617.1.
    AK162844 mRNA. Translation: BAE37078.1.
    BC065106 mRNA. Translation: AAH65106.1.
    BC065143 mRNA. Translation: AAH65143.1.
    CCDSiCCDS17874.1.
    PIRiA53444.
    RefSeqiNP_001264145.1. NM_001277216.1.
    NP_001264146.1. NM_001277217.1.
    NP_001264147.1. NM_001277218.1.
    NP_001264149.1. NM_001277220.1.
    NP_031586.1. NM_007560.4.
    XP_006501002.1. XM_006500939.1.
    XP_006501003.1. XM_006500940.1.
    XP_006501004.1. XM_006500941.1.
    XP_006501005.1. XM_006500942.1.
    XP_006501006.1. XM_006500943.1.
    XP_006501007.1. XM_006500944.1.
    XP_006501008.1. XM_006500945.1.
    UniGeneiMm.39089.

    Genome annotation databases

    EnsembliENSMUST00000029948; ENSMUSP00000029948; ENSMUSG00000052430.
    ENSMUST00000098568; ENSMUSP00000096167; ENSMUSG00000052430.
    ENSMUST00000106230; ENSMUSP00000101837; ENSMUSG00000052430.
    ENSMUST00000106232; ENSMUSP00000101839; ENSMUSG00000052430.
    GeneIDi12167.
    KEGGimmu:12167.
    UCSCiuc008rog.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z23143 mRNA. Translation: CAA80674.1 .
    AK086130 mRNA. Translation: BAC39617.1 .
    AK162844 mRNA. Translation: BAE37078.1 .
    BC065106 mRNA. Translation: AAH65106.1 .
    BC065143 mRNA. Translation: AAH65143.1 .
    CCDSi CCDS17874.1.
    PIRi A53444.
    RefSeqi NP_001264145.1. NM_001277216.1.
    NP_001264146.1. NM_001277217.1.
    NP_001264147.1. NM_001277218.1.
    NP_001264149.1. NM_001277220.1.
    NP_031586.1. NM_007560.4.
    XP_006501002.1. XM_006500939.1.
    XP_006501003.1. XM_006500940.1.
    XP_006501004.1. XM_006500941.1.
    XP_006501005.1. XM_006500942.1.
    XP_006501006.1. XM_006500943.1.
    XP_006501007.1. XM_006500944.1.
    XP_006501008.1. XM_006500945.1.
    UniGenei Mm.39089.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EVS X-ray 2.10 C 14-126 [» ]
    ProteinModelPortali P36898.
    SMRi P36898. Positions 29-113, 174-500.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-252N.
    IntActi P36898. 1 interaction.
    MINTi MINT-124245.

    PTM databases

    PhosphoSitei P36898.

    Proteomic databases

    PaxDbi P36898.
    PRIDEi P36898.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029948 ; ENSMUSP00000029948 ; ENSMUSG00000052430 .
    ENSMUST00000098568 ; ENSMUSP00000096167 ; ENSMUSG00000052430 .
    ENSMUST00000106230 ; ENSMUSP00000101837 ; ENSMUSG00000052430 .
    ENSMUST00000106232 ; ENSMUSP00000101839 ; ENSMUSG00000052430 .
    GeneIDi 12167.
    KEGGi mmu:12167.
    UCSCi uc008rog.1. mouse.

    Organism-specific databases

    CTDi 658.
    MGIi MGI:107191. Bmpr1b.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000110337.
    HOGENOMi HOG000230587.
    HOVERGENi HBG054502.
    InParanoidi P36898.
    KOi K13578.
    OMAi LRCKCHH.
    OrthoDBi EOG7Q8CN3.
    PhylomeDBi P36898.
    TreeFami TF314724.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3474.
    Reactomei REACT_220505. Signaling by BMP.

    Miscellaneous databases

    ChiTaRSi BMPR1B. mouse.
    EvolutionaryTracei P36898.
    NextBioi 280535.
    PROi P36898.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P36898.
    Bgeei P36898.
    CleanExi MM_BMPR1B.
    Genevestigatori P36898.

    Family and domain databases

    InterProi IPR000472. Activin_rcpt.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    IPR003605. TGF_beta_rcpt_GS.
    IPR000333. TGFB_receptor.
    [Graphical view ]
    PANTHERi PTHR23255. PTHR23255. 1 hit.
    Pfami PF01064. Activin_recp. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF08515. TGF_beta_GS. 1 hit.
    [Graphical view ]
    SMARTi SM00467. GS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51256. GS. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of type I receptors for transforming growth factor-beta and activin."
      ten Dijke P., Yamashita H., Ichijo H., Franzen P., Laiho M., Miyazono K., Heldin C.-H.
      Science 264:101-104(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Head and Hypothalamus.
    3. "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].
      Strain: C57BL/6.
      Tissue: Brain and Retina.
    4. "Crystal structure analysis reveals a spring-loaded latch as molecular mechanism for GDF-5-type I receptor specificity."
      Kotzsch A., Nickel J., Seher A., Sebald W., Muller T.D.
      EMBO J. 28:937-947(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 14-126 IN COMPLEX WITH HUMAN GDF5, DISULFIDE BONDS.

    Entry informationi

    Entry nameiBMR1B_MOUSE
    AccessioniPrimary (citable) accession number: P36898
    Secondary accession number(s): Q3TRF2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 143 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3