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O00238

- BMR1B_HUMAN

UniProt

O00238 - BMR1B_HUMAN

Protein

Bone morphogenetic protein receptor type-1B

Gene

BMPR1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      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: HGNC
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. protein serine/threonine kinase activity Source: HGNC
    5. receptor signaling protein serine/threonine kinase activity Source: InterPro
    6. SMAD binding Source: HGNC
    7. transforming growth factor beta receptor activity, type I Source: Ensembl
    8. transmembrane receptor protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. BMP signaling pathway Source: UniProtKB
    2. cartilage condensation Source: UniProtKB
    3. chondrocyte differentiation Source: Ensembl
    4. dorsal/ventral pattern formation Source: Ensembl
    5. eye development Source: UniProtKB
    6. inflammatory response Source: Ensembl
    7. limb morphogenesis Source: UniProtKB
    8. ovarian cumulus expansion Source: UniProtKB
    9. ovulation cycle Source: UniProtKB
    10. positive regulation of bone mineralization Source: BHF-UCL
    11. positive regulation of cell differentiation Source: UniProtKB
    12. positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
    13. positive regulation of osteoblast differentiation Source: BHF-UCL
    14. protein phosphorylation Source: HGNC
    15. retina development in camera-type eye Source: Ensembl
    16. retinal ganglion cell axon guidance Source: Ensembl
    17. skeletal system development Source: UniProtKB

    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. 2681.
    ReactomeiREACT_12034. Signaling by BMP.
    SignaLinkiO00238.

    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):
    CD_antigen: CDw293
    Gene namesi
    Name:BMPR1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:1077. BMPR1B.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of plasma membrane Source: UniProtKB
    2. plasma membrane Source: Reactome
    3. receptor complex Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Acromesomelic chondrodysplasia, with genital anomalies (AMDGA) [MIM:609441]: A form of chondrodysplasia. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers).1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Brachydactyly A2 (BDA2) [MIM:112600]: A form of brachydactyly. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. In brachydactyly type A2 shortening of the middle phalanges is confined to the index finger and the second toe, all other digits being more or less normal. Because of a rhomboid or triangular shape of the affected middle phalanx, the end of the second finger usually deviates radially.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti200 – 2001I → K in BDA2. 1 Publication
    Corresponds to variant rs28939703 [ dbSNP | Ensembl ].
    VAR_023819
    Natural varianti486 – 4861R → Q in brachydactyly type C and BDA2; with also additional features of symphalangism-1. 1 Publication
    VAR_037967
    Natural varianti486 – 4861R → W in BDA2. 1 Publication
    Corresponds to variant rs28939704 [ dbSNP | Ensembl ].
    VAR_023820

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi112600. phenotype.
    609441. phenotype.
    Orphaneti93396. Brachydactyly type A2.
    93384. Brachydactyly type C.
    PharmGKBiPA25387.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1313Sequence AnalysisAdd
    BLAST
    Chaini14 – 502489Bone morphogenetic protein receptor type-1BPRO_0000024412Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi32 ↔ 53By similarity
    Disulfide bondi34 ↔ 38By similarity
    Disulfide bondi47 ↔ 71By similarity
    Disulfide bondi81 ↔ 95By similarity
    Disulfide bondi96 ↔ 102By similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiO00238.
    PaxDbiO00238.
    PRIDEiO00238.

    PTM databases

    PhosphoSiteiO00238.

    Expressioni

    Gene expression databases

    ArrayExpressiO00238.
    BgeeiO00238.
    CleanExiHS_BMPR1B.
    GenevestigatoriO00238.

    Organism-specific databases

    HPAiCAB009634.
    HPA046821.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BMP2P126433EBI-7527193,EBI-1029262
    GDF5P430266EBI-7527193,EBI-8571476

    Protein-protein interaction databases

    BioGridi107126. 68 interactions.
    IntActiO00238. 3 interactions.
    MINTiMINT-1340235.
    STRINGi9606.ENSP00000264568.

    Structurei

    Secondary structure

    1
    502
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi176 – 18611
    Beta strandi190 – 1923
    Helixi194 – 1974
    Helixi200 – 2034
    Beta strandi205 – 2139
    Beta strandi216 – 2238
    Beta strandi226 – 2349
    Helixi235 – 2373
    Helixi238 – 24811
    Beta strandi261 – 2688
    Helixi270 – 2723
    Beta strandi274 – 2796
    Helixi287 – 2937
    Helixi298 – 31619
    Beta strandi337 – 3404
    Beta strandi346 – 3483
    Helixi375 – 3773
    Helixi380 – 3834
    Helixi393 – 41119
    Turni426 – 4305
    Helixi437 – 4448
    Helixi455 – 4595
    Helixi461 – 47313
    Helixi478 – 4803
    Helixi484 – 49613
    Turni497 – 4993

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MDYX-ray2.05A/C168-502[»]
    ProteinModelPortaliO00238.
    SMRiO00238. Positions 29-113, 174-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00238.

    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.
    HOGENOMiHOG000230587.
    HOVERGENiHBG054502.
    InParanoidiO00238.
    KOiK13578.
    OMAiLRCKCHH.
    OrthoDBiEOG7Q8CN3.
    PhylomeDBiO00238.
    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]
    PRINTSiPR00653. ACTIVIN2R.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00238-1) [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

    MLLRSAGKLN VGTKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD    50
    GYCFTMIEED DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN 100
    ECNKDLHPTL PPLKNRDFVD GPIHHRALLI SVTVCSLLLV LIILFCYFRY 150
    KRQETRPRYS 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
    YSFGLILWEV ARRCVSGGIV EEYQLPYHDL VPSDPSYEDM REIVCIKKLR 450
    PSFPNRWSSD ECLRQMGKLM TECWAHNPAS RLTALRVKKT LAKMSESQDI 500
    KL 502
    Length:502
    Mass (Da):56,930
    Last modified:July 1, 1997 - v1
    Checksum:iB283D9BF45535C79
    GO
    Isoform 2 (identifier: O00238-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MGWLEELNWQLHIFLLILLSMHTRANFLDNM

    Show »
    Length:532
    Mass (Da):60,582
    Checksum:i5DF28FF01C96D541
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311R → H in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041401
    Natural varianti149 – 1491R → W.1 Publication
    Corresponds to variant rs34231464 [ dbSNP | Ensembl ].
    VAR_041402
    Natural varianti200 – 2001I → K in BDA2. 1 Publication
    Corresponds to variant rs28939703 [ dbSNP | Ensembl ].
    VAR_023819
    Natural varianti224 – 2241R → H.1 Publication
    Corresponds to variant rs35973133 [ dbSNP | Ensembl ].
    VAR_041403
    Natural varianti297 – 2971D → N in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_041404
    Natural varianti371 – 3711R → Q.1 Publication
    Corresponds to variant rs34970181 [ dbSNP | Ensembl ].
    VAR_041405
    Natural varianti486 – 4861R → Q in brachydactyly type C and BDA2; with also additional features of symphalangism-1. 1 Publication
    VAR_037967
    Natural varianti486 – 4861R → W in BDA2. 1 Publication
    Corresponds to variant rs28939704 [ dbSNP | Ensembl ].
    VAR_023820

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MGWLEELNWQLHIFLLILLS MHTRANFLDNM in isoform 2. 1 PublicationVSP_045100

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89675 mRNA. Translation: BAA19765.1.
    U89326 mRNA. Translation: AAC28131.1.
    AK299930 mRNA. Translation: BAG61763.1.
    AK313642 mRNA. Translation: BAG36400.1.
    AC004061 Genomic DNA. No translation available.
    AC092609 Genomic DNA. No translation available.
    AC093634 Genomic DNA. No translation available.
    AC105395 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX06060.1.
    BC047773 mRNA. Translation: AAH47773.1.
    BC069796 mRNA. Translation: AAH69796.1.
    BC069803 mRNA. Translation: AAH69803.1.
    CCDSiCCDS3642.1. [O00238-1]
    CCDS58919.1. [O00238-2]
    RefSeqiNP_001194.1. NM_001203.2. [O00238-1]
    NP_001243721.1. NM_001256792.1. [O00238-1]
    NP_001243722.1. NM_001256793.1. [O00238-2]
    NP_001243723.1. NM_001256794.1. [O00238-1]
    XP_006714355.1. XM_006714292.1. [O00238-1]
    UniGeneiHs.598475.

    Genome annotation databases

    EnsembliENST00000264568; ENSP00000264568; ENSG00000138696. [O00238-1]
    ENST00000394931; ENSP00000378389; ENSG00000138696. [O00238-1]
    ENST00000440890; ENSP00000401907; ENSG00000138696. [O00238-2]
    ENST00000509540; ENSP00000421671; ENSG00000138696. [O00238-1]
    ENST00000512312; ENSP00000425444; ENSG00000138696. [O00238-1]
    ENST00000515059; ENSP00000426617; ENSG00000138696. [O00238-1]
    GeneIDi658.
    KEGGihsa:658.
    UCSCiuc003htm.4. human. [O00238-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89675 mRNA. Translation: BAA19765.1 .
    U89326 mRNA. Translation: AAC28131.1 .
    AK299930 mRNA. Translation: BAG61763.1 .
    AK313642 mRNA. Translation: BAG36400.1 .
    AC004061 Genomic DNA. No translation available.
    AC092609 Genomic DNA. No translation available.
    AC093634 Genomic DNA. No translation available.
    AC105395 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX06060.1 .
    BC047773 mRNA. Translation: AAH47773.1 .
    BC069796 mRNA. Translation: AAH69796.1 .
    BC069803 mRNA. Translation: AAH69803.1 .
    CCDSi CCDS3642.1. [O00238-1 ]
    CCDS58919.1. [O00238-2 ]
    RefSeqi NP_001194.1. NM_001203.2. [O00238-1 ]
    NP_001243721.1. NM_001256792.1. [O00238-1 ]
    NP_001243722.1. NM_001256793.1. [O00238-2 ]
    NP_001243723.1. NM_001256794.1. [O00238-1 ]
    XP_006714355.1. XM_006714292.1. [O00238-1 ]
    UniGenei Hs.598475.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MDY X-ray 2.05 A/C 168-502 [» ]
    ProteinModelPortali O00238.
    SMRi O00238. Positions 29-113, 174-500.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107126. 68 interactions.
    IntActi O00238. 3 interactions.
    MINTi MINT-1340235.
    STRINGi 9606.ENSP00000264568.

    Chemistry

    BindingDBi O00238.
    ChEMBLi CHEMBL5476.
    GuidetoPHARMACOLOGYi 1789.

    PTM databases

    PhosphoSitei O00238.

    Proteomic databases

    MaxQBi O00238.
    PaxDbi O00238.
    PRIDEi O00238.

    Protocols and materials databases

    DNASUi 658.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264568 ; ENSP00000264568 ; ENSG00000138696 . [O00238-1 ]
    ENST00000394931 ; ENSP00000378389 ; ENSG00000138696 . [O00238-1 ]
    ENST00000440890 ; ENSP00000401907 ; ENSG00000138696 . [O00238-2 ]
    ENST00000509540 ; ENSP00000421671 ; ENSG00000138696 . [O00238-1 ]
    ENST00000512312 ; ENSP00000425444 ; ENSG00000138696 . [O00238-1 ]
    ENST00000515059 ; ENSP00000426617 ; ENSG00000138696 . [O00238-1 ]
    GeneIDi 658.
    KEGGi hsa:658.
    UCSCi uc003htm.4. human. [O00238-1 ]

    Organism-specific databases

    CTDi 658.
    GeneCardsi GC04P095679.
    HGNCi HGNC:1077. BMPR1B.
    HPAi CAB009634.
    HPA046821.
    MIMi 112600. phenotype.
    603248. gene.
    609441. phenotype.
    neXtProti NX_O00238.
    Orphaneti 93396. Brachydactyly type A2.
    93384. Brachydactyly type C.
    PharmGKBi PA25387.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000230587.
    HOVERGENi HBG054502.
    InParanoidi O00238.
    KOi K13578.
    OMAi LRCKCHH.
    OrthoDBi EOG7Q8CN3.
    PhylomeDBi O00238.
    TreeFami TF314724.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_12034. Signaling by BMP.
    SignaLinki O00238.

    Miscellaneous databases

    ChiTaRSi BMPR1B. human.
    EvolutionaryTracei O00238.
    GeneWikii BMPR1B.
    GenomeRNAii 658.
    NextBioi 2676.
    PROi O00238.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00238.
    Bgeei O00238.
    CleanExi HS_BMPR1B.
    Genevestigatori O00238.

    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 ]
    PRINTSi PR00653. ACTIVIN2R.
    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. "Cloning of human bone morphogenetic protein type IB receptor (BMPR-IB) and its expression in prostate cancer in comparison with other BMPRs."
      Ide H., Katoh M., Sasaki H., Yoshida T., Aoki K., Nawa Y., Osada Y., Sugimura T., Terada M.
      Oncogene 14:1377-1382(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Prostate.
    2. "Chromosomal localization of three human genes encoding bone morphogenetic protein receptors."
      Astroem A.-K., Jin D.F., Imamura T., Roijer E., Rosenzweig B., Miyazono K., ten Dijke P., Stenman G.
      Mamm. Genome 10:299-302(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Ovary.
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Uterus.
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1).
      Tissue: PNS.
    7. Cited for: VARIANTS BDA2 LYS-200 AND TRP-486.
    8. "A homozygous BMPR1B mutation causes a new subtype of acromesomelic chondrodysplasia with genital anomalies."
      Demirhan O., Tuerkmen S., Schwabe G.C., Soyupak S., Akguel E., Tastemir D., Karahan D., Mundlos S., Lehmann K.
      J. Med. Genet. 42:314-317(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN AMDGA.
    9. "A novel R486Q mutation in BMPR1B resulting in either a brachydactyly type C/symphalangism-like phenotype or brachydactyly type A2."
      Lehmann K., Seemann P., Boergermann J., Morin G., Reif S., Knaus P., Mundlos S.
      Eur. J. Hum. Genet. 14:1248-1254(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BRACHYDACTYLY TYPE C/BDA2 GLN-486.
    10. "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] HIS-31; TRP-149; HIS-224; ASN-297 AND GLN-371.

    Entry informationi

    Entry nameiBMR1B_HUMAN
    AccessioniPrimary (citable) accession number: O00238
    Secondary accession number(s): B2R953, B4DSV1, P78366
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 157 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3