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O00238

- BMR1B_HUMAN

UniProt

O00238 - BMR1B_HUMAN

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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

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 serine/threonine kinase activity Source: HGNC
  4. receptor signaling protein serine/threonine kinase activity Source: InterPro
  5. SMAD binding Source: HGNC
  6. transforming growth factor beta receptor activity, type I Source: Ensembl
  7. 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
Complete GO annotation...

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
Complete GO annotation...

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.
Orphaneti2098. Acromesomelic dysplasia, Grebe type.
93396. 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

BgeeiO00238.
CleanExiHS_BMPR1B.
ExpressionAtlasiO00238. baseline and differential.
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. 69 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 – 18611Combined sources
Beta strandi190 – 1923Combined sources
Helixi194 – 1974Combined sources
Helixi200 – 2034Combined sources
Beta strandi205 – 2139Combined sources
Beta strandi216 – 2238Combined sources
Beta strandi226 – 2349Combined sources
Helixi235 – 2373Combined sources
Helixi238 – 24811Combined sources
Beta strandi261 – 2688Combined sources
Helixi270 – 2723Combined sources
Beta strandi274 – 2796Combined sources
Helixi287 – 2937Combined sources
Helixi298 – 31619Combined sources
Beta strandi337 – 3404Combined sources
Beta strandi346 – 3483Combined sources
Helixi375 – 3773Combined sources
Helixi380 – 3834Combined sources
Helixi393 – 41119Combined sources
Turni426 – 4305Combined sources
Helixi437 – 4448Combined sources
Helixi455 – 4595Combined sources
Helixi461 – 47313Combined sources
Helixi478 – 4803Combined sources
Helixi484 – 49613Combined sources
Turni497 – 4993Combined sources

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.
GeneTreeiENSGT00760000118876.
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

        10         20         30         40         50
MLLRSAGKLN VGTKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD
60 70 80 90 100
GYCFTMIEED DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN
110 120 130 140 150
ECNKDLHPTL PPLKNRDFVD GPIHHRALLI SVTVCSLLLV LIILFCYFRY
160 170 180 190 200
KRQETRPRYS IGLEQDETYI PPGESLRDLI EQSQSSGSGS GLPLLVQRTI
210 220 230 240 250
AKQIQMVKQI GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS WFRETEIYQT
260 270 280 290 300
VLMRHENILG FIAADIKGTG SWTQLYLITD YHENGSLYDY LKSTTLDAKS
310 320 330 340 350
MLKLAYSSVS GLCHLHTEIF STQGKPAIAH RDLKSKNILV KKNGTCCIAD
360 370 380 390 400
LGLAVKFISD TNEVDIPPNT RVGTKRYMPP EVLDESLNRN HFQSYIMADM
410 420 430 440 450
YSFGLILWEV ARRCVSGGIV EEYQLPYHDL VPSDPSYEDM REIVCIKKLR
460 470 480 490 500
PSFPNRWSSD ECLRQMGKLM TECWAHNPAS RLTALRVKKT LAKMSESQDI

KL
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. 69 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 2098. Acromesomelic dysplasia, Grebe type.
93396. Brachydactyly type A2.
93384. Brachydactyly type C.
PharmGKBi PA25387.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118876.
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

Bgeei O00238.
CleanExi HS_BMPR1B.
ExpressionAtlasi O00238. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 158 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