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P36898 (BMR1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bone morphogenetic protein receptor type-1B

Short name=BMP type-1B receptor
Short name=BMPR-1B
EC=2.7.11.30
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 names
Name:Bmpr1b
Synonyms:Acvrlk6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Magnesium or manganese By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.

Contains 1 GS domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processChondrogenesis
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from mutant phenotype PubMed 11376112. Source: MGI

cartilage condensation

Inferred from mutant phenotype PubMed 10631181. Source: MGI

chondrocyte differentiation

Inferred from genetic interaction PubMed 18363966. Source: MGI

dorsal/ventral pattern formation

Inferred from genetic interaction PubMed 15673568. Source: MGI

estrogen biosynthetic process

Non-traceable author statement PubMed 11416163. Source: UniProtKB

inflammatory response

Inferred from expression pattern PubMed 12151307. Source: UniProtKB

limb morphogenesis

Inferred from electronic annotation. Source: Ensembl

ovarian cumulus expansion

Inferred from mutant phenotype PubMed 11416163. Source: UniProtKB

positive regulation of bone mineralization

Inferred from electronic annotation. Source: Ensembl

positive regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from genetic interaction PubMed 18363966. Source: MGI

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

retina development in camera-type eye

Inferred from mutant phenotype PubMed 12654290. Source: MGI

retinal ganglion cell axon guidance

Inferred from mutant phenotype PubMed 12654290. Source: MGI

transforming growth factor beta receptor signaling pathway

Traceable author statement PubMed 10631181. Source: MGI

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta receptor activity, type I

Inferred from mutant phenotype PubMed 11376112. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Smad6O351822EBI-7107883,EBI-4321242

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1313 Potential
Chain14 – 502489Bone morphogenetic protein receptor type-1B
PRO_0000024413

Regions

Topological domain14 – 126113Extracellular Potential
Transmembrane127 – 14822Helical; Potential
Topological domain149 – 502354Cytoplasmic Potential
Domain174 – 20330GS
Domain204 – 494291Protein kinase
Nucleotide binding210 – 2189ATP By similarity

Sites

Active site3321Proton acceptor By similarity
Binding site2311ATP By similarity

Amino acid modifications

Disulfide bond32 ↔ 53 Ref.4
Disulfide bond34 ↔ 38 Ref.4
Disulfide bond47 ↔ 71 Ref.4
Disulfide bond81 ↔ 95 Ref.4
Disulfide bond96 ↔ 102 Ref.4

Secondary structure

............... 502
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36898 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: AB29681F3FF5A361

FASTA50256,944
        10         20         30         40         50         60 
MLLRSSGKLN VGTKKEDGES TAPTPRPKIL RCKCHHHCPE DSVNNICSTD GYCFTMIEED 

        70         80         90        100        110        120 
DSGMPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKDRDFVD 

       130        140        150        160        170        180 
GPIHHKALLI SVTVCSLLLV LIILFCYFRY KRQEARPRYS IGLEQDETYI PPGESLRDLI 

       190        200        210        220        230        240 
EQSQSSGSGS GLPLLVQRTI AKQIQMVKQI GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS 

       250        260        270        280        290        300 
WFRETEIYQT VLMRHENILG FIAADIKGTG SWTQLYLITD YHENGSLYDY LKSTTLDAKS 

       310        320        330        340        350        360 
MLKLAYSSVS GLCHLHTEIF STQGKPAIAH RDLKSKNILV KKNGTCCIAD LGLAVKFISD 

       370        380        390        400        410        420 
TNEVDIPPNT RVGTKRYMPP EVLDESLNRN HFQSYIMADM YSFGLILWEI ARRCVSGGIV 

       430        440        450        460        470        480 
EEYQLPYHDL VPSDPSYEDM REIVCMKKLR PSFPNRWSSD ECLRQMGKLM TECWAQNPAS 

       490        500 
RLTALRVKKT LAKMSESQDI KL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA53444.
RefSeqNP_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.
UniGeneMm.39089.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EVSX-ray2.10C14-126[»]
ProteinModelPortalP36898.
SMRP36898. Positions 29-113, 174-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-252N.
IntActP36898. 1 interaction.
MINTMINT-124245.

PTM databases

PhosphoSiteP36898.

Proteomic databases

PaxDbP36898.
PRIDEP36898.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029948; ENSMUSP00000029948; ENSMUSG00000052430.
ENSMUST00000098568; ENSMUSP00000096167; ENSMUSG00000052430.
ENSMUST00000106230; ENSMUSP00000101837; ENSMUSG00000052430.
ENSMUST00000106232; ENSMUSP00000101839; ENSMUSG00000052430.
GeneID12167.
KEGGmmu:12167.
UCSCuc008rog.1. mouse.

Organism-specific databases

CTD658.
MGIMGI:107191. Bmpr1b.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110337.
HOGENOMHOG000230587.
HOVERGENHBG054502.
InParanoidP36898.
KOK13578.
OMALRCKCHH.
OrthoDBEOG7Q8CN3.
TreeFamTF314724.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.

Gene expression databases

ArrayExpressP36898.
BgeeP36898.
CleanExMM_BMPR1B.
GenevestigatorP36898.

Family and domain databases

InterProIPR000472. 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.
[Graphical view]
PfamPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
SMARTSM00467. GS. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBMPR1B. mouse.
EvolutionaryTraceP36898.
NextBio280535.
PROP36898.
SOURCESearch...

Entry information

Entry nameBMR1B_MOUSE
AccessionPrimary (citable) accession number: P36898
Secondary accession number(s): Q3TRF2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: March 19, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot