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O00238 (BMR1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. 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·Alt products·Sequence annotation·Sequences·References·Web links·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):
CD_antigen=CDw293
Gene names
Name:BMPR1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.

Involvement in disease

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).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

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
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Dwarfism
   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

Non-traceable author statement Ref.2. Source: UniProtKB

cartilage condensation

Non-traceable author statement Ref.7. Source: UniProtKB

chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

dorsal/ventral pattern formation

Inferred from electronic annotation. Source: Ensembl

eye development

Inferred from sequence or structural similarity. Source: UniProtKB

inflammatory response

Inferred from electronic annotation. Source: Ensembl

limb morphogenesis

Inferred from mutant phenotype Ref.7. Source: UniProtKB

ovarian cumulus expansion

Inferred from sequence or structural similarity. Source: UniProtKB

ovulation cycle

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of bone mineralization

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

positive regulation of cell differentiation

Inferred from mutant phenotype Ref.7. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast differentiation

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

protein phosphorylation

Inferred from direct assay PubMed 12065756. Source: HGNC

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

retinal ganglion cell axon guidance

Inferred from electronic annotation. Source: Ensembl

skeletal system development

Inferred from mutant phenotype Ref.7. Source: UniProtKB

   Cellular_componentintegral component of plasma membrane

Inferred by curator Ref.7. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

receptor complex

Traceable author statement Ref.7. Source: UniProtKB

   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 serine/threonine kinase activity

Inferred from direct assay PubMed 12065756. Source: HGNC

receptor signaling protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

transforming growth factor beta receptor activity, type I

Inferred from electronic annotation. Source: Ensembl

transmembrane receptor protein serine/threonine kinase activity

Inferred from mutant phenotype Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00238-1)

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.
Isoform 2 (identifier: O00238-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1313 Potential
Chain14 – 502489Bone morphogenetic protein receptor type-1B
PRO_0000024412

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 By similarity
Disulfide bond34 ↔ 38 By similarity
Disulfide bond47 ↔ 71 By similarity
Disulfide bond81 ↔ 95 By similarity
Disulfide bond96 ↔ 102 By similarity

Natural variations

Alternative sequence11M → MGWLEELNWQLHIFLLILLS MHTRANFLDNM in isoform 2.
VSP_045100
Natural variant311R → H in a gastric adenocarcinoma sample; somatic mutation. Ref.10
VAR_041401
Natural variant1491R → W. Ref.10
Corresponds to variant rs34231464 [ dbSNP | Ensembl ].
VAR_041402
Natural variant2001I → K in BDA2. Ref.7
Corresponds to variant rs28939703 [ dbSNP | Ensembl ].
VAR_023819
Natural variant2241R → H. Ref.10
Corresponds to variant rs35973133 [ dbSNP | Ensembl ].
VAR_041403
Natural variant2971D → N in a metastatic melanoma sample; somatic mutation. Ref.10
VAR_041404
Natural variant3711R → Q. Ref.10
Corresponds to variant rs34970181 [ dbSNP | Ensembl ].
VAR_041405
Natural variant4861R → Q in brachydactyly type C and BDA2; with also additional features of symphalangism-1. Ref.9
VAR_037967
Natural variant4861R → W in BDA2. Ref.7
Corresponds to variant rs28939704 [ dbSNP | Ensembl ].
VAR_023820

Secondary structure

.................................................. 502
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: B283D9BF45535C79

FASTA50256,930
        10         20         30         40         50         60 
MLLRSAGKLN VGTKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD GYCFTMIEED 

        70         80         90        100        110        120 
DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKNRDFVD 

       130        140        150        160        170        180 
GPIHHRALLI SVTVCSLLLV LIILFCYFRY KRQETRPRYS 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 YSFGLILWEV ARRCVSGGIV 

       430        440        450        460        470        480 
EEYQLPYHDL VPSDPSYEDM REIVCIKKLR PSFPNRWSSD ECLRQMGKLM TECWAHNPAS 

       490        500 
RLTALRVKKT LAKMSESQDI KL 

« Hide

Isoform 2 [UniParc].

Checksum: 5DF28FF01C96D541
Show »

FASTA53260,582

References

« Hide 'large scale' references
[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. 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] (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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Mutations in bone morphogenetic protein receptor 1B cause brachydactyly type A2."
Lehmann K., Seemann P., Stricker S., Sammar M., Meyer B., Suering K., Majewski F., Tinschert S., Grzeschik K.-H., Mueller D., Knaus P., Nuernberg P., Mundlos S.
Proc. Natl. Acad. Sci. U.S.A. 100:12277-12282(2003) [PubMed] [Europe PMC] [Abstract]
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. 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] HIS-31; TRP-149; HIS-224; ASN-297 AND GLN-371.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001194.1. NM_001203.2.
NP_001243721.1. NM_001256792.1.
NP_001243722.1. NM_001256793.1.
NP_001243723.1. NM_001256794.1.
UniGeneHs.598475.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MDYX-ray2.05A/C168-502[»]
ProteinModelPortalO00238.
SMRO00238. Positions 29-113, 174-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107126. 67 interactions.
IntActO00238. 3 interactions.
MINTMINT-1340235.
STRING9606.ENSP00000264568.

Chemistry

BindingDBO00238.
ChEMBLCHEMBL5476.
GuidetoPHARMACOLOGY1789.

PTM databases

PhosphoSiteO00238.

Proteomic databases

PaxDbO00238.
PRIDEO00238.

Protocols and materials databases

DNASU658.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264568; 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]
GeneID658.
KEGGhsa:658.
UCSCuc003htm.4. human. [O00238-1]

Organism-specific databases

CTD658.
GeneCardsGC04P095679.
HGNCHGNC:1077. BMPR1B.
HPACAB009634.
HPA046821.
MIM112600. phenotype.
603248. gene.
609441. phenotype.
neXtProtNX_O00238.
Orphanet93396. Brachydactyly type A2.
93384. Brachydactyly type C.
PharmGKBPA25387.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000230587.
HOVERGENHBG054502.
InParanoidO00238.
KOK13578.
OMALRCKCHH.
OrthoDBEOG7Q8CN3.
PhylomeDBO00238.
TreeFamTF314724.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111102. Signal Transduction.
SignaLinkO00238.

Gene expression databases

ArrayExpressO00238.
BgeeO00238.
CleanExHS_BMPR1B.
GenevestigatorO00238.

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]
PfamPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
PRINTSPR00653. ACTIVIN2R.
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. human.
EvolutionaryTraceO00238.
GeneWikiBMPR1B.
GenomeRNAi658.
NextBio2676.
PROO00238.
SOURCESearch...

Entry information

Entry nameBMR1B_HUMAN
AccessionPrimary (citable) accession number: O00238
Secondary accession number(s): B2R953, B4DSV1, P78366
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 152 of the entry and version 1 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 4

Human chromosome 4: entries, gene names and cross-references to MIM

Human cell differentiation molecules

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