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Protein

Bone morphogenetic protein receptor type-1B

Gene

Bmpr1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. Positively regulates chondrocyte differentiation through GDF5 interaction (PubMed:24098149).1 Publication

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+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

GO - Biological processi

  • BMP signaling pathway Source: MGI
  • camera-type eye development Source: MGI
  • cartilage condensation Source: MGI
  • cell differentiation Source: MGI
  • chondrocyte development Source: AgBase
  • chondrocyte differentiation Source: UniProtKB
  • dorsal/ventral pattern formation Source: MGI
  • endochondral bone morphogenesis Source: AgBase
  • estrogen biosynthetic process Source: UniProtKB
  • eye development Source: MGI
  • inflammatory response Source: UniProtKB
  • limb morphogenesis Source: MGI
  • negative regulation of chondrocyte proliferation Source: AgBase
  • ovarian cumulus expansion Source: UniProtKB
  • ovulation cycle Source: UniProtKB
  • positive regulation of bone mineralization Source: MGI
  • positive regulation of cartilage development Source: AgBase
  • positive regulation of cell differentiation Source: MGI
  • positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  • positive regulation of osteoblast differentiation Source: MGI
  • protein phosphorylation Source: MGI
  • proteoglycan biosynthetic process Source: AgBase
  • retina development in camera-type eye Source: MGI
  • retinal ganglion cell axon guidance Source: MGI
  • skeletal system development Source: MGI
  • transforming growth factor beta receptor signaling pathway Source: MGI
  • transmembrane receptor protein serine/threonine kinase signaling pathway Source: MGI
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. 3474.
ReactomeiREACT_334226. 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 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:107191. Bmpr1b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini14 – 126113ExtracellularSequence AnalysisAdd
BLAST
Transmembranei127 – 14822HelicalSequence AnalysisAdd
BLAST
Topological domaini149 – 502354CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

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

BgeeiP36898.
CleanExiMM_BMPR1B.
ExpressionAtlasiP36898. baseline and differential.
GenevisibleiP36898. MM.

Interactioni

Subunit structurei

Interacts with high affinity with GDF5; positively regulates chondrocyte differentiation.By similarity

Binary interactionsi

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

Protein-protein interaction databases

DIPiDIP-252N.
IntActiP36898. 1 interaction.
MINTiMINT-124245.
STRINGi10090.ENSMUSP00000029948.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP36898.

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.
InParanoidiP36898.
KOiK13578.
OMAiLRCKCHH.
OrthoDBiEOG7Q8CN3.
PhylomeDBiP36898.
TreeFamiTF314724.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR000472. TFB_recept_I/II_C.
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

        10         20         30         40         50
MLLRSSGKLN VGTKKEDGES TAPTPRPKIL RCKCHHHCPE DSVNNICSTD
60 70 80 90 100
GYCFTMIEED DSGMPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN
110 120 130 140 150
ECNKDLHPTL PPLKDRDFVD GPIHHKALLI SVTVCSLLLV LIILFCYFRY
160 170 180 190 200
KRQEARPRYS 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
YSFGLILWEI ARRCVSGGIV EEYQLPYHDL VPSDPSYEDM REIVCMKKLR
460 470 480 490 500
PSFPNRWSSD ECLRQMGKLM TECWAQNPAS RLTALRVKKT LAKMSESQDI

KL
Length:502
Mass (Da):56,944
Last modified:June 1, 1994 - v1
Checksum:iAB29681F3FF5A361
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006500939.2.
XP_006501003.1. XM_006500940.2.
XP_006501004.1. XM_006500941.2.
XP_006501005.1. XM_006500942.1.
XP_006501006.1. XM_006500943.2.
XP_006501007.1. XM_006500944.2.
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:
EMBLi
GenBanki
DDBJi
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_006500939.2.
XP_006501003.1. XM_006500940.2.
XP_006501004.1. XM_006500941.2.
XP_006501005.1. XM_006500942.1.
XP_006501006.1. XM_006500943.2.
XP_006501007.1. XM_006500944.2.
UniGeneiMm.39089.

3D structure databases

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

Protein-protein interaction databases

DIPiDIP-252N.
IntActiP36898. 1 interaction.
MINTiMINT-124245.
STRINGi10090.ENSMUSP00000029948.

PTM databases

PhosphoSiteiP36898.

Proteomic databases

PaxDbiP36898.
PRIDEiP36898.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi658.
MGIiMGI:107191. Bmpr1b.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118876.
HOGENOMiHOG000230587.
HOVERGENiHBG054502.
InParanoidiP36898.
KOiK13578.
OMAiLRCKCHH.
OrthoDBiEOG7Q8CN3.
PhylomeDBiP36898.
TreeFamiTF314724.

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_334226. Signaling by BMP.

Miscellaneous databases

ChiTaRSiBmpr1b. mouse.
EvolutionaryTraceiP36898.
NextBioi280535.
PROiP36898.
SOURCEiSearch...

Gene expression databases

BgeeiP36898.
CleanExiMM_BMPR1B.
ExpressionAtlasiP36898. baseline and differential.
GenevisibleiP36898. MM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR000472. TFB_recept_I/II_C.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: FUNCTION.
  5. "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: June 24, 2015
This is version 151 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.