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Reviewed, UniProtKB/Swiss-Prot Q13705 (AVR2B_HUMAN)

Last modified November 25, 2008. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Activin receptor type-2B
    EC=2.7.11.30
Alternative name(s):
    Activin receptor type IIB
      Short name=ACTR-IIB
Gene names
Name: ACVR2B
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length512 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 activin A, activin B and inhibin A.

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

Defects in ACVR2B are a cause of left-right axis malformations [MIM:602730]. Th effect is due to the loss of normal left-right asymmetry. Complete left-right asymmetry reversal imparts no deleterious consequences to the affected individual, whereas randomization typically results in complex, often lethal heart malformations as well as abdominal abnormalities.

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords

   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainSignal
Transmembrane
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMGlycoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processBMP signaling pathway

Inferred from direct assay. Source: UniProtKB

anterior/posterior pattern formation Ref.3

Inferred from mutant phenotype. Source: HGNC

positive regulation of activin receptor signaling pathway

Inferred from direct assay. Source: HGNC

positive regulation of bone mineralization

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of osteoblast differentiation

Inferred from mutant phenotype. Source: UniProtKB

protein amino acid phosphorylation

Inferred from electronic annotation. Source: InterPro

regulation of transcription

Inferred from direct assay. Source: HGNC

   Cellular componentcell surface

Inferred from direct assay. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HGNC

integral to plasma membrane Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionATP binding

Inferred from electronic annotation. Source: InterPro

activin receptor activity

Inferred from electronic annotation. Source: InterPro

growth factor binding

Inferred from physical interaction. Source: HGNC

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Select]
Isoform ActR-IIB2 (identifier: Q13705-1)

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 ActR-IIB1 (identifier: Q13705-2)

The sequence of this isoform is not available.
Notes: Produced from the insertion in the transcript of 82 base pairs, leading to frameshift and protein truncation. May be not functional.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 512494Activin receptor type-2B
PRO_0000024404

Regions

Topological domain19 – 137119Extracellular Potential
Transmembrane138 – 15821 Potential
Topological domain159 – 512354Cytoplasmic Potential
Domain190 – 480291Protein kinase
Nucleotide binding196 – 2049ATP By similarity

Sites

Active site3211Proton acceptor By similarity
Binding site2171ATP By similarity

Amino acid modifications

Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation651N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 59 By similarity
Disulfide bond49 ↔ 77 By similarity
Disulfide bond84 ↔ 103 By similarity
Disulfide bond90 ↔ 102 By similarity
Disulfide bond104 ↔ 109 By similarity

Natural variations

Natural variant401R → H in left-right axis malformations.
VAR_013281
Natural variant1761P → R
VAR_041396
Natural variant4941V → I in left-right axis malformations.
VAR_013282

Experimental info

Sequence conflict16 – 172CA → WP in CAA54671. Ref.1
Sequence conflict641R → A Ref.1 Ref.2
Sequence conflict4591E → A in AAC64515. Ref.3
Sequence conflict4591E → D in BAA24180. Ref.2

Secondary structure

..................................................................... 512
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform ActR-IIB2 [UniParc].

Last modified May 16, 2006. Version 3.
Checksum: B377FEF92EF74937

FASTA51257,724
        10         20         30         40         50         60 
MTAPWVALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GEQDKRLHCY 

        70         80         90        100        110        120 
ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEAG 

       130        140        150        160        170        180 
GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP 

       190        200        210        220        230        240 
PSPLVGLKPL QLLEIKARGR FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK 

       250        260        270        280        290        300 
HENLLQFIAA EKRGSNLEVE LWLITAFHDK GSLTDYLKGN IITWNELCHV AETMSRGLSY 

       310        320        330        340        350        360 
LHEDVPWCRG EGHKPSIAHR DFKSKNVLLK SDLTAVLADF GLAVRFEPGK PPGDTHGQVG 

       370        380        390        400        410        420 
TRRYMAPEVL EGAINFQRDA FLRIDMYAMG LVLWELVSRC KAADGPVDEY MLPFEEEIGQ 

       430        440        450        460        470        480 
HPSLEELQEV VVHKKMRPTI KDHWLKHPGL AQLCVTIEEC WDHDAEARLS AGCVEERVSL 

       490        500        510 
IRRSVNGTTS DCLVSLVTSV TNVDLPPKES SI 

« Hide

Isoform ActR-IIB1 (Sequence not available).

References

« Hide 'large scale' references
[1]"Expression of type II activin receptor genes during differentiation of human K562 cells and cDNA cloning of the human type IIB activin receptor."
Hilden K., Tuuri T., Eramaa M., Ritvos O.
Blood 83:2163-2170(1994) [PubMed: 8161782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Genomic organization and mapping of the human activin receptor type IIB (hActR-IIB) gene."
Ishikawa S., Kai M., Murata Y., Tamari M., Daigo Y., Murano T., Ogawa M., Nakamura Y.
J. Hum. Genet. 43:132-134(1998) [PubMed: 9621519] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Left-right axis malformations associated with mutations in ACVR2B, the gene for human activin receptor type IIB."
Kosaki R., Gebbia M., Kosaki K., Lewin M., Bowers P., Towbin J.A., Casey B.
Am. J. Med. Genet. 82:70-76(1999) [PubMed: 9916847] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, VARIANTS LEFT-RIGHT AXIS MALFORMATIONS HIS-40 AND ILE-494.
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"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: 17344846] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-176.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

X77533 mRNA. Translation: CAA54671.1.
AB008681 Genomic DNA. Translation: BAA24180.2.
AF060202 expand/collapse EMBL AC list , AF060199, AF060200, AF060201 Genomic DNA. Translation: AAC64515.1.
BC096243 mRNA. Translation: AAH96243.1.
BC096244 mRNA. Translation: AAH96244.1.
BC099642 mRNA. Translation: AAH99642.1.
PIRI37134.
RefSeq