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P36894 (BMR1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 176. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | 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-1A

Short name=BMP type-1A receptor
Short name=BMPR-1A
EC=2.7.11.30
Alternative name(s):
Activin receptor-like kinase 3
Short name=ALK-3
Serine/threonine-protein kinase receptor R5
Short name=SKR5
CD_antigen=CD292
Gene names
Name:BMPR1A
Synonyms:ACVRLK3, ALK3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length532 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 BMP-2 and BMP-4.

Catalytic activity

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

Cofactor

Magnesium or manganese By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Highly expressed in skeletal muscle.

Involvement in disease

Juvenile polyposis syndrome (JPS) [MIM:174900]: Autosomal dominant gastrointestinal hamartomatous polyposis syndrome in which patients are at risk for developing gastrointestinal cancers. The lesions are typified by a smooth histological appearance, predominant stroma, cystic spaces and lack of a smooth muscle core. Multiple juvenile polyps usually occur in a number of Mendelian disorders. Sometimes, these polyps occur without associated features as in JPS; here, polyps tend to occur in the large bowel and are associated with an increased risk of colon and other gastrointestinal cancers.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Polyposis syndrome, mixed hereditary 2 (HMPS2) [MIM:610069]: A disease is characterized by atypical juvenile polyps, colonic adenomas, and colorectal carcinomas.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

A microdeletion of chromosome 10q23 involving BMPR1A and PTEN is a cause of chromosome 10q23 deletion syndrome, which shows overlapping features of the following three disorders: Bannayan-Zonana syndrome, Cowden disease and juvenile polyposis syndrome. Ref.6

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

Inferred from direct assay PubMed 18436533PubMed 9389648. Source: BHF-UCL

Mullerian duct regression

Inferred from electronic annotation. Source: Ensembl

cartilage development

Inferred from electronic annotation. Source: Ensembl

developmental growth

Inferred from electronic annotation. Source: Ensembl

dorsal/ventral axis specification

Inferred from electronic annotation. Source: Ensembl

ectoderm development

Inferred from electronic annotation. Source: Ensembl

embryonic digit morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic organ development

Inferred from electronic annotation. Source: Ensembl

endocardial cushion formation

Inferred from sequence or structural similarity. Source: BHF-UCL

heart formation

Inferred from electronic annotation. Source: Ensembl

hindlimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

immune response

Inferred from mutant phenotype PubMed 16886151. Source: BHF-UCL

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

lateral mesoderm development

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

mesendoderm development

Inferred from electronic annotation. Source: Ensembl

mesoderm formation

Inferred from electronic annotation. Source: Ensembl

negative regulation of neurogenesis

Inferred from electronic annotation. Source: Ensembl

neural crest cell development

Inferred from electronic annotation. Source: Ensembl

neural plate mediolateral regionalization

Inferred from electronic annotation. Source: Ensembl

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

palate development

Inferred from electronic annotation. Source: Ensembl

paraxial mesoderm structural organization

Inferred from electronic annotation. Source: Ensembl

pituitary gland development

Inferred from electronic annotation. Source: Ensembl

positive regulation of SMAD protein import into nucleus

Inferred from direct assay PubMed 9389648. Source: BHF-UCL

positive regulation of bone mineralization

Inferred from mutant phenotype PubMed 18436533. Source: BHF-UCL

positive regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of mesenchymal cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 18436533. Source: BHF-UCL

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from direct assay PubMed 9389648. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay PubMed 12065756. Source: HGNC

regulation of lateral mesodermal cell fate specification

Inferred from electronic annotation. Source: Ensembl

somitogenesis

Inferred from electronic annotation. Source: Ensembl

stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentdendrite

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Traceable author statement Ref.1. Source: ProtInc

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 15657086. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from direct assay PubMed 12065756. Source: HGNC

SMAD binding

Inferred from direct assay PubMed 12065756. Source: HGNC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 11278302. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 18436533. Source: BHF-UCL

protein serine/threonine kinase activity

Inferred from direct assay PubMed 12065756. Source: HGNC

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta-activated receptor activity

Inferred from electronic annotation. Source: InterPro

transmembrane receptor protein serine/threonine kinase activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 532509Bone morphogenetic protein receptor type-1A
PRO_0000024410

Regions

Topological domain24 – 152129Extracellular Potential
Transmembrane153 – 17624Helical; Potential
Topological domain177 – 532356Cytoplasmic Potential
Domain204 – 23330GS
Domain234 – 525292Protein kinase
Nucleotide binding240 – 2489ATP By similarity
Region107 – 1093Mediates specificity for BMP ligand

Sites

Active site3621Proton acceptor By similarity
Binding site2611ATP By similarity

Amino acid modifications

Glycosylation731N-linked (GlcNAc...) Potential
Disulfide bond61 ↔ 82
Disulfide bond63 ↔ 67
Disulfide bond76 ↔ 100
Disulfide bond110 ↔ 124
Disulfide bond125 ↔ 130

Natural variations

Natural variant21P → T. Ref.1 Ref.2 Ref.13
Corresponds to variant rs11528010 [ dbSNP | Ensembl ].
VAR_041397
Natural variant581F → Y in a renal clear cell carcinoma sample; somatic mutation. Ref.13
VAR_041398
Natural variant621Y → D in JPS. Ref.8
VAR_022828
Natural variant821C → Y in JPS. Ref.8
VAR_022829
Natural variant1241C → R in JPS. Ref.7
VAR_015533
Natural variant1301C → R in JPS. Ref.9
VAR_022830
Natural variant3381A → D in JPS. Ref.7
VAR_015534
Natural variant3761C → Y in JPS. Ref.7
VAR_015535
Natural variant4431R → C in JPS. Ref.8 Ref.13
Corresponds to variant rs35619497 [ dbSNP | Ensembl ].
VAR_022831
Natural variant4501V → M. Ref.13
Corresponds to variant rs55932635 [ dbSNP | Ensembl ].
VAR_041399
Natural variant4701M → T in JPS. Ref.10
VAR_022832
Natural variant4861R → Q in a gastric adenocarcinoma sample; somatic mutation. Ref.13
VAR_041400

Experimental info

Mutagenesis107 – 1093DFQ → REL: Affinity for BMP2 decreased by over 200-fold. Ref.4

Secondary structure

................... 532
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36894 [UniParc].

Last modified March 15, 2005. Version 2.
Checksum: 00CE2DDDA3A44170

FASTA53260,198
        10         20         30         40         50         60 
MPQLYIYIRL LGAYLFIISR VQGQNLDSML HGTGMKSDSD QKKSENGVTL APEDTLPFLK 

        70         80         90        100        110        120 
CYCSGHCPDD AINNTCITNG HCFAIIEEDD QGETTLASGC MKYEGSDFQC KDSPKAQLRR 

       130        140        150        160        170        180 
TIECCRTNLC NQYLQPTLPP VVIGPFFDGS IRWLVLLISM AVCIIAMIIF SSCFCYKHYC 

       190        200        210        220        230        240 
KSISSRRRYN RDLEQDEAFI PVGESLKDLI DQSQSSGSGS GLPLLVQRTI AKQIQMVRQV 

       250        260        270        280        290        300 
GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS WFRETEIYQT VLMRHENILG FIAADIKGTG 

       310        320        330        340        350        360 
SWTQLYLITD YHENGSLYDF LKCATLDTRA LLKLAYSAAC GLCHLHTEIY GTQGKPAIAH 

       370        380        390        400        410        420 
RDLKSKNILI KKNGSCCIAD LGLAVKFNSD TNEVDVPLNT RVGTKRYMAP EVLDESLNKN 

       430        440        450        460        470        480 
HFQPYIMADI YSFGLIIWEM ARRCITGGIV EEYQLPYYNM VPSDPSYEDM REVVCVKRLR 

       490        500        510        520        530 
PIVSNRWNSD ECLRAVLKLM SECWAHNPAS RLTALRIKKT LAKMVESQDV KI 

« Hide

References

« Hide 'large scale' references
[1]"Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity."
ten Dijke P., Ichijo H., Franzen P., Schulz P., Saras J., Toyoshima H., Heldin C.-H., Miyazono K.
Oncogene 8:2879-2887(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-2.
Tissue: Placenta.
[2]"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. expand/collapse author list , 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], VARIANT THR-2.
Tissue: Placenta.
[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].
Tissue: Testis.
[4]"Structure of the Alk1 extracellular domain and characterization of its bone morphogenetic protein (BMP) binding properties."
Mahlawat P., Ilangovan U., Biswas T., Sun L.Z., Hinck A.P.
Biochemistry 51:6328-6341(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BMP2, MUTAGENESIS OF 107-ASP--GLN-109.
[5]"Crystal structure of the BMP-2-BRIA ectodomain complex."
Kirsch T., Sebald W., Dreyer M.K.
Nat. Struct. Biol. 7:492-496(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 55-143 IN COMPLEX WITH BMP-2.
[6]"Germline mutations of the gene encoding bone morphogenetic protein receptor 1A in juvenile polyposis."
Howe J.R., Bair J.L., Sayed M.G., Anderson M.E., Mitros F.A., Petersen G.M., Velculescu V.E., Traverso G., Vogelstein B.
Nat. Genet. 28:184-187(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[7]"Germline mutations in BMPR1A/ALK3 cause a subset of cases of juvenile polyposis syndrome and of Cowden and Bannayan-Riley-Ruvalcaba syndromes."
Zhou X.-P., Woodford-Richens K., Lehtonen R., Kurose K., Aldred M., Hampel H., Launonen V., Virta S., Pilarski R., Salovaara R., Bodmer W.F., Conrad B.A., Dunlop M., Hodgson S.V., Iwama T., Jaervinen H., Kellokumpu I., Kim J.C. expand/collapse author list , Leggett B., Markie D., Mecklin J.-P., Neale K., Phillips R., Piris J., Rozen P., Houlston R.S., Aaltonen L.A., Tomlinson I.P.M., Eng C.
Am. J. Hum. Genet. 69:704-711(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS JPS ARG-124; ASP-338 AND TYR-376.
[8]"Germline SMAD4 or BMPR1A mutations and phenotype of juvenile polyposis."
Sayed M.G., Ahmed A.F., Ringold J.R., Anderson M.E., Bair J.L., Mitros F.A., Lynch H.T., Tinley S.T., Petersen G.M., Giardiello F.M., Vogelstein B., Howe J.R.
Ann. Surg. Oncol. 9:901-906(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS JPS ASP-62; TYR-82 AND CYS-443.
[9]"Juvenile polyposis: massive gastric polyposis is more common in MADH4 mutation carriers than in BMPR1A mutation carriers."
Friedl W., Uhlhaas S., Schulmann K., Stolte M., Loff S., Back W., Mangold E., Stern M., Knaebel H.P., Sutter C., Weber R.G., Pistorius S., Burger B., Propping P.
Hum. Genet. 111:108-111(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT JPS ARG-130.
[10]"Identification of a novel BMPR1A germline mutation in a Korean juvenile polyposis patient without SMAD4 mutation."
Kim I.J., Park J.H., Kang H.C., Kim K.H., Kim J.H., Ku J.L., Kang S.B., Park S.Y., Lee J.S., Park J.G.
Clin. Genet. 63:126-130(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT JPS THR-470.
[11]"Contiguous gene deletion within chromosome arm 10q is associated with juvenile polyposis of infancy, reflecting cooperation between the BMPR1A and PTEN tumor-suppressor genes."
Delnatte C., Sanlaville D., Mougenot J.-F., Vermeesch J.-R., Houdayer C., Blois M.-C., Genevieve D., Goulet O., Fryns J.-P., Jaubert F., Vekemans M., Lyonnet S., Romana S., Eng C., Stoppa-Lyonnet D.
Am. J. Hum. Genet. 78:1066-1074(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN JUVENILE POLYPOSIS OF INFANCY.
[12]"Mapping of hereditary mixed polyposis syndrome (HMPS) to chromosome 10q23 by genomewide high-density single nucleotide polymorphism (SNP) scan and identification of BMPR1A loss of function."
Cao X., Eu K.W., Kumarasinghe M.P., Li H.H., Loi C., Cheah P.Y.
J. Med. Genet. 43:E13-E13(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HEREDITARY MIXED POLYPOSIS SYNDROME 2.
[13]"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. expand/collapse author list , 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] THR-2; TYR-58; CYS-443; MET-450 AND GLN-486.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z22535 mRNA. Translation: CAA80257.1.
AK291764 mRNA. Translation: BAF84453.1.
BC028383 mRNA. Translation: AAH28383.1.
CCDSCCDS7378.1.
PIRI37163.
RefSeqNP_004320.2. NM_004329.2.
UniGeneHs.524477.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ES7X-ray2.90B/D55-143[»]
1REWX-ray1.86C/D24-152[»]
2GOOX-ray2.20B/E24-152[»]
2H62X-ray1.85C24-152[»]
2H64X-ray1.92B24-152[»]
2K3GNMR-A51-152[»]
2QJ9X-ray2.44C/D24-152[»]
2QJAX-ray2.60C/D24-152[»]
2QJBX-ray2.50C/D24-152[»]
3NH7X-ray2.70A/B/C/D24-152[»]
3QB4X-ray2.28B/D24-152[»]
ProteinModelPortalP36894.
SMRP36894. Positions 57-140, 204-530.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107125. 33 interactions.
DIPDIP-5793N.
IntActP36894. 7 interactions.
MINTMINT-124304.
STRING9606.ENSP00000224764.

Chemistry

BindingDBP36894.
ChEMBLCHEMBL5275.
GuidetoPHARMACOLOGY1786.

PTM databases

PhosphoSiteP36894.

Polymorphism databases

DMDM61252444.

Proteomic databases

MaxQBP36894.
PaxDbP36894.
PRIDEP36894.

Protocols and materials databases

DNASU657.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372037; ENSP00000361107; ENSG00000107779.
GeneID657.
KEGGhsa:657.
UCSCuc001kdy.3. human.

Organism-specific databases

CTD657.
GeneCardsGC10P088506.
GeneReviewsBMPR1A.
HGNCHGNC:1076. BMPR1A.
HPACAB019398.
MIM174900. phenotype.
601299. gene.
610069. phenotype.
612242. phenotype.
neXtProtNX_P36894.
Orphanet329971. Generalized juvenile polyposis/juvenile polyposis coli.
157794. Hereditary mixed polyposis syndrome.
144. Hereditary nonpolyposis colon cancer.
79076. Juvenile polyposis of infancy.
PharmGKBPA25386.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000230587.
HOVERGENHBG054502.
InParanoidP36894.
KOK04673.
OMACYNRDLE.
OrthoDBEOG7Q8CN3.
PhylomeDBP36894.
TreeFamTF314724.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111102. Signal Transduction.
SignaLinkP36894.

Gene expression databases

BgeeP36894.
CleanExHS_BMPR1A.
GenevestigatorP36894.

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.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERPTHR23255. PTHR23255. 1 hit.
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

EvolutionaryTraceP36894.
GeneWikiBMPR1A.
GenomeRNAi657.
NextBio2672.
PROP36894.
SOURCESearch...

Entry information

Entry nameBMR1A_HUMAN
AccessionPrimary (citable) accession number: P36894
Secondary accession number(s): A8K6U9, Q8NEN8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: March 15, 2005
Last modified: July 9, 2014
This is version 176 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries