[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; PubMed=8161782 [NCBI, ExPASy, EBI, Israel, Japan] Hilden K., Tuuri T., Eramaa M., Ritvos O.; "Expression of type II activin receptor genes during differentiation of human K562 cells and cDNA cloning of the human type IIB activin receptor."; Blood 83:2163-2170(1994).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/s100380050054; PubMed=9621519 [NCBI, ExPASy, EBI, Israel, Japan] Ishikawa S., Kai M., Murata Y., Tamari M., Daigo Y., Murano T., Ogawa M., Nakamura Y.; "Genomic organization and mapping of the human activin receptor type IIB (hActR-IIB) gene."; J. Hum. Genet. 43:132-134(1998).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANTS LEFT-RIGHT AXIS MALFORMATIONS HIS-40 AND ILE-494. DOI=10.1002/(SICI)1096-8628(19990101)82:1<70::AID-AJMG14>3.0.CO;2-Y; PubMed=9916847 [NCBI, ExPASy, EBI, Israel, Japan] Kosaki R., Gebbia M., Kosaki K., Lewin M., Bowers P., Towbin J.A., Casey B.; "Left-right axis malformations associated with mutations in ACVR2B, the gene for human activin receptor type IIB."; Am. J. Med. Genet. 82:70-76(1999).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	VARIANT [LARGE SCALE ANALYSIS] ARG-176. DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan] 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., 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.; "Patterns of somatic mutation in human cancer genomes."; Nature 446:153-158(2007).

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.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	ActR-IIB2
Isoform ID	Q13705-1
This is the isoform sequence displayed in this entry.

Name	ActR-IIB1
Isoform ID	Q13705-2
Note: Produced from the insertion in the transcript of 82 base pairs, leading to frameshift and protein truncation. May be not functional.
The sequence of this isoform is not described.

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.
SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.
SIMILARITY: Contains 1 protein kinase domain.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=ACVR2B";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X77533; CAA54671.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB008681; BAA24180.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF060202; AAC64515.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF060199; AAC64515.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF060200; AAC64515.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF060201; AAC64515.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC096243; AAH96243.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC096244; AAH96244.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC099642; AAH99642.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

I37134; I37134.

NP_001097.2; -.

3D structure databases

PDB

2H62; X-ray; 1.85 A; D=19-116.

[ExPASy / RCSB / EBI]

PDBsum

2H62; -.

ModBase

Q13705.

Protein-protein interaction databases

IntAct

Q13705; -.

Organism-specific databases

HGNC:174; ACVR2B.

602730; gene+phenotype. [NCBI / EBI]

PharmGKB

PA24495; -.

GeneCards

Q13705.

Gene expression databases

ArrayExpress

Q13705; -.

CleanEx

HS_ACVR2B; -.

GermOnline

ENSG00000114739; Homo sapiens.

Ontologies

GO:0009986;	Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from HGNC).
GO:0005887;	Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0019838;	Molecular function: growth factor binding (inferred from physical interaction from HGNC).
GO:0004674;	Molecular function: protein serine/threonine kinase activity (inferred from mutant phenotype from HGNC).
GO:0009952;	Biological process: anterior/posterior pattern formation (inferred from mutant phenotype from HGNC).
GO:0030509;	Biological process: BMP signaling pathway (inferred from direct assay from UniProtKB).
GO:0032927;	Biological process: positive regulation of activin receptor signaling pathway (inferred from direct assay from HGNC).
GO:0030501;	Biological process: positive regulation of bone mineralization (inferred from mutant phenotype from UniProtKB).
GO:0045669;	Biological process: positive regulation of osteoblast differentiation (inferred from mutant phenotype from UniProtKB).
GO:0045449;	Biological process: regulation of transcription (inferred from direct assay from HGNC).
QuickGo view.

Family and domain databases

InterPro

IPR000333; Activin_II_recpt.
IPR015768; Activin_II_recpt_C.
IPR000472; Activin_rcpt.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.

PANTHER

PTHR23255:SF10; Activin_II_recpt_C; 1.

Pfam

PF01064; Activin_recp; 1.
PF00069; Pkinase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00653; ACTIVIN2R.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q13705.

Genome annotation databases

Ensembl

ENSG00000114739; Homo sapiens. [Contig view]

GeneID

93; -.

KEGG

hsa:93; -.

Phylogenomic databases

HOVERGEN

Q13705; -.

Other

SOURCE

ACVR2B; Homo sapiens.

ProtoNet

Q13705.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; ATP-binding; Disease mutation; Glycoprotein; Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; Polymorphism; Receptor; Serine/threonine-protein kinase; Signal; Transferase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`	`Potential.`
`CHAIN`	`19 512`	`494`	`Activin receptor type-2B.`	`PRO_0000024404`
`TOPO_DOM`	`19 137`	`119`	`Extracellular (Potential).`
`TRANSMEM`	`138 158`	`21`	`Potential.`
`TOPO_DOM`	`159 512`	`354`	`Cytoplasmic (Potential).`
`DOMAIN`	`190 480`	`291`	`Protein kinase.`
`NP_BIND`	`196 204`	`9`	`ATP (By similarity).`
`ACT_SITE`	`321 321`		`Proton acceptor (By similarity).`
`BINDING`	`217 217`		`ATP (By similarity).`
`CARBOHYD`	`42 42`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`65 65`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`29 59`		`By similarity.`
`DISULFID`	`49 77`		`By similarity.`
`DISULFID`	`84 103`		`By similarity.`
`DISULFID`	`90 102`		`By similarity.`
`DISULFID`	`104 109`		`By similarity.`
`VARIANT`	`40 40`	`1`	`R -> H (in left-right axis malformations).`	`VAR_013281`
`VARIANT`	`176 176`	`1`	`P -> R.`	`VAR_041396`
`VARIANT`	`494 494`	`1`	`V -> I (in left-right axis malformations).`	`VAR_013282`
`CONFLICT`	`16 17`		`CA -> WP (in Ref. 1; CAA54671).`
`CONFLICT`	`64 64`		`R -> A (in Ref. 1 and 2).`
`CONFLICT`	`459 459`		`E -> A (in Ref. 3; AAC64515).`
`CONFLICT`	`459 459`		`E -> D (in Ref. 2; BAA24180).`
`STRAND`	`191 197`	`7`
`STRAND`	`200 209`	`10`
`STRAND`	`212 219`	`8`
`HELIX`	`221 223`	`3`
`HELIX`	`224 235`	`12`
`STRAND`	`247 253`	`7`
`TURN`	`256 258`	`3`
`STRAND`	`260 266`	`7`
`HELIX`	`273 279`	`7`
`HELIX`	`284 302`	`19`
`STRAND`	`305 308`	`4`
`TURN`	`309 311`	`3`
`STRAND`	`312 314`	`3`
`STRAND`	`316 318`	`3`
`HELIX`	`324 326`	`3`
`STRAND`	`327 329`	`3`
`STRAND`	`335 337`	`3`
`STRAND`	`344 346`	`3`
`HELIX`	`362 364`	`3`
`HELIX`	`367 370`	`4`
`HELIX`	`378 398`	`21`
`TURN`	`413 417`	`5`
`HELIX`	`424 431`	`8`
`HELIX`	`442 446`	`5`
`HELIX`	`448 460`	`13`
`HELIX`	`465 467`	`3`
`HELIX`	`471 482`	`12`

Sequence information

Length: 512 AA [This is the length of the unprocessed precursor]

Molecular weight: 57724 Da [This is the MW of the unprocessed precursor]

CRC64: B377FEF92EF74937 [This is a checksum on the sequence]

        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

Q13705 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools