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Database: UniProt
Entry: AVR2B_HUMAN
LinkDB: AVR2B_HUMAN
Original site: AVR2B_HUMAN 
ID   AVR2B_HUMAN             Reviewed;         512 AA.
AC   Q13705; Q4VAV0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 3.
DT   27-MAR-2024, entry version 225.
DE   RecName: Full=Activin receptor type-2B;
DE            EC=2.7.11.30;
DE   AltName: Full=Activin receptor type IIB;
DE            Short=ACTR-IIB;
DE   Flags: Precursor;
GN   Name=ACVR2B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=8161782;
RA   Hilden K., Tuuri T., Eramaa M., Ritvos O.;
RT   "Expression of type II activin receptor genes during differentiation of
RT   human K562 cells and cDNA cloning of the human type IIB activin receptor.";
RL   Blood 83:2163-2170(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASP-459.
RX   PubMed=9621519; DOI=10.1007/s100380050054;
RA   Ishikawa S., Kai M., Murata Y., Tamari M., Daigo Y., Murano T., Ogawa M.,
RA   Nakamura Y.;
RT   "Genomic organization and mapping of the human activin receptor type IIB
RT   (hActR-IIB) gene.";
RL   J. Hum. Genet. 43:132-134(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANTS HTX4
RP   HIS-40 AND ILE-494.
RX   PubMed=9916847;
RX   DOI=10.1002/(sici)1096-8628(19990101)82:1<70::aid-ajmg14>3.0.co;2-y;
RA   Kosaki R., Gebbia M., Kosaki K., Lewin M., Bowers P., Towbin J.A.,
RA   Casey B.;
RT   "Left-right axis malformations associated with mutations in ACVR2B, the
RT   gene for human activin receptor type IIB.";
RL   Am. J. Med. Genet. 82:70-76(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION, INTERACTION WITH ACVR1B, AND FUNCTION IN PHOSPHORYLATION
RP   OF ACVR1B.
RX   PubMed=8622651; DOI=10.1128/mcb.16.3.1066;
RA   Attisano L., Wrana J.L., Montalvo E., Massague J.;
RT   "Activation of signalling by the activin receptor complex.";
RL   Mol. Cell. Biol. 16:1066-1073(1996).
RN   [6]
RP   INTERACTION WITH VPS39.
RX   PubMed=12941698; DOI=10.1093/emboj/cdg428;
RA   Felici A., Wurthner J.U., Parks W.T., Giam L.R., Reiss M., Karpova T.S.,
RA   McNally J.G., Roberts A.B.;
RT   "TLP, a novel modulator of TGF-beta signaling, has opposite effects on
RT   Smad2- and Smad3-dependent signaling.";
RL   EMBO J. 22:4465-4477(2003).
RN   [7]
RP   INTERACTION WITH BMP6.
RX   PubMed=18070108; DOI=10.1111/j.1742-4658.2007.06187.x;
RA   Saremba S., Nickel J., Seher A., Kotzsch A., Sebald W., Mueller T.D.;
RT   "Type I receptor binding of bone morphogenetic protein 6 is dependent on N-
RT   glycosylation of the ligand.";
RL   FEBS J. 275:172-183(2008).
RN   [8]
RP   INTERACTION WITH BMP3, AND SUBCELLULAR LOCATION.
RX   PubMed=31665064; DOI=10.1186/s13046-019-1435-1;
RA   Wen J., Liu X., Qi Y., Niu F., Niu Z., Geng W., Zou Z., Huang R., Wang J.,
RA   Zou H.;
RT   "BMP3 suppresses colon tumorigenesis via ActRIIB/SMAD2-dependent and
RT   TAK1/JNK signaling pathways.";
RL   J. Exp. Clin. Cancer Res. 38:428-428(2019).
RN   [9] {ECO:0007744|PDB:2H62}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 19-116, AND INTERACTION WITH
RP   BMP2.
RX   PubMed=17295905; DOI=10.1186/1472-6807-7-6;
RA   Weber D., Kotzsch A., Nickel J., Harth S., Seher A., Mueller U., Sebald W.,
RA   Mueller T.D.;
RT   "A silent H-bond can be mutationally activated for high-affinity
RT   interaction of BMP-2 and activin type IIB receptor.";
RL   BMC Struct. Biol. 7:6-6(2007).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.36 ANGSTROMS) OF 19-134 IN COMPLEX WITH ACVRL1 AND
RP   BMP9, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-42 AND ASN-65.
RX   PubMed=22718755; DOI=10.1074/jbc.m112.377960;
RA   Townson S.A., Martinez-Hackert E., Greppi C., Lowden P., Sako D., Liu J.,
RA   Ucran J.A., Liharska K., Underwood K.W., Seehra J., Kumar R.,
RA   Grinberg A.V.;
RT   "Specificity and structure of a high affinity activin receptor-like kinase
RT   1 (ALK1) signaling complex.";
RL   J. Biol. Chem. 287:27313-27325(2012).
RN   [11]
RP   VARIANT [LARGE SCALE ANALYSIS] ARG-176.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Transmembrane serine/threonine kinase activin type-2 receptor
CC       forming an activin receptor complex with activin type-1
CC       serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces
CC       the activin signal from the cell surface to the cytoplasm and is thus
CC       regulating many physiological and pathological processes including
CC       neuronal differentiation and neuronal survival, hair follicle
CC       development and cycling, FSH production by the pituitary gland, wound
CC       healing, extracellular matrix production, immunosuppression and
CC       carcinogenesis. Activin is also thought to have a paracrine or
CC       autocrine role in follicular development in the ovary. Within the
CC       receptor complex, the type-2 receptors act as a primary activin
CC       receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-
CC       A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream
CC       transducers of activin signals. Activin binds to type-2 receptor at the
CC       plasma membrane and activates its serine-threonine kinase. The
CC       activated receptor type-2 then phosphorylates and activates the type-1
CC       receptor. Once activated, the type-1 receptor binds and phosphorylates
CC       the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal
CC       tail. Soon after their association with the activin receptor and
CC       subsequent phosphorylation, SMAD2 and SMAD3 are released into the
CC       cytoplasm where they interact with the common partner SMAD4. This SMAD
CC       complex translocates into the nucleus where it mediates activin-induced
CC       transcription. Inhibitory SMAD7, which is recruited to ACVR1B through
CC       FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin
CC       receptor complex, thereby blocking the activin signal. Activin signal
CC       transduction is also antagonized by the binding to the receptor of
CC       inhibin-B via the IGSF1 inhibin coreceptor.
CC       {ECO:0000269|PubMed:8622651}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC         L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC         COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC         ChEBI:CHEBI:456216; EC=2.7.11.30;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC         seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC         Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.30;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Forms an activin receptor complex with activin type II
CC       receptors such as ACVR1B. Interacts with VPS39. Interacts with DYNLT1.
CC       Interacts with BMP3 (PubMed:31665064). Interacts with BMP2
CC       (PubMed:17295905). Interacts with BMP6 (PubMed:18070108).
CC       {ECO:0000250|UniProtKB:P27040, ECO:0000269|PubMed:12941698,
CC       ECO:0000269|PubMed:17295905, ECO:0000269|PubMed:18070108,
CC       ECO:0000269|PubMed:22718755, ECO:0000269|PubMed:31665064,
CC       ECO:0000269|PubMed:8622651}.
CC   -!- INTERACTION:
CC       Q13705; O14793: MSTN; NbExp=4; IntAct=EBI-1383577, EBI-8542977;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31665064};
CC       Single-pass type I membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=ActR-IIB2;
CC         IsoId=Q13705-1; Sequence=Displayed;
CC       Name=ActR-IIB1;
CC         IsoId=Q13705-2; Sequence=Not described;
CC   -!- PTM: Phosphorylated. Constitutive phosphorylation is in part catalyzed
CC       by its own kinase activity. {ECO:0000269|PubMed:8622651}.
CC   -!- DISEASE: Heterotaxy, visceral, 4, autosomal (HTX4) [MIM:613751]: A form
CC       of visceral heterotaxy, a complex disorder due to disruption of the
CC       normal left-right asymmetry of the thoracoabdominal organs. Visceral
CC       heterotaxy or situs ambiguus results in randomization of the placement
CC       of visceral organs, including the heart, lungs, liver, spleen, and
CC       stomach. The organs are oriented randomly with respect to the left-
CC       right axis and with respect to one another. It can be associated with a
CC       variety of congenital defects including cardiac malformations. HTX4
CC       clinical features include dextrocardia, right aortic arch and a right-
CC       sided spleen, anomalies of the inferior and the superior vena cava,
CC       atrial ventricular canal defect with dextro-transposed great arteries,
CC       pulmonary stenosis, polysplenia and midline liver.
CC       {ECO:0000269|PubMed:9916847}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform ActR-IIB1]: Produced from the insertion in the
CC       transcript of 82 base pairs, leading to frameshift and protein
CC       truncation. May be not functional. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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DR   EMBL; X77533; CAA54671.1; -; mRNA.
DR   EMBL; AB008681; BAA24180.2; -; Genomic_DNA.
DR   EMBL; AF060202; AAC64515.1; -; Genomic_DNA.
DR   EMBL; AF060199; AAC64515.1; JOINED; Genomic_DNA.
DR   EMBL; AF060200; AAC64515.1; JOINED; Genomic_DNA.
DR   EMBL; AF060201; AAC64515.1; JOINED; Genomic_DNA.
DR   EMBL; BC096243; AAH96243.1; -; mRNA.
DR   EMBL; BC096244; AAH96244.1; -; mRNA.
DR   EMBL; BC099642; AAH99642.1; -; mRNA.
DR   CCDS; CCDS2679.1; -. [Q13705-1]
DR   PIR; I37134; I37134.
DR   RefSeq; NP_001097.2; NM_001106.3. [Q13705-1]
DR   PDB; 2H62; X-ray; 1.85 A; D=19-116.
DR   PDB; 2QLU; X-ray; 2.00 A; A=190-487.
DR   PDB; 4FAO; X-ray; 3.36 A; E/F/K/L/Q/R/W/X/e/f/k/l=19-134.
DR   PDB; 5NGV; X-ray; 2.00 A; A=24-117.
DR   PDB; 5NHR; X-ray; 3.35 A; C/D=24-117.
DR   PDB; 7MRZ; X-ray; 3.00 A; C=19-134.
DR   PDB; 7OLY; X-ray; 3.27 A; C=19-134.
DR   PDBsum; 2H62; -.
DR   PDBsum; 2QLU; -.
DR   PDBsum; 4FAO; -.
DR   PDBsum; 5NGV; -.
DR   PDBsum; 5NHR; -.
DR   PDBsum; 7MRZ; -.
DR   PDBsum; 7OLY; -.
DR   AlphaFoldDB; Q13705; -.
DR   SMR; Q13705; -.
DR   BioGRID; 106608; 100.
DR   IntAct; Q13705; 31.
DR   MINT; Q13705; -.
DR   STRING; 9606.ENSP00000340361; -.
DR   BindingDB; Q13705; -.
DR   ChEMBL; CHEMBL5466; -.
DR   DrugCentral; Q13705; -.
DR   GuidetoPHARMACOLOGY; 1792; -.
DR   GlyCosmos; Q13705; 2 sites, No reported glycans.
DR   GlyGen; Q13705; 2 sites.
DR   iPTMnet; Q13705; -.
DR   PhosphoSitePlus; Q13705; -.
DR   BioMuta; ACVR2B; -.
DR   DMDM; 97535735; -.
DR   EPD; Q13705; -.
DR   jPOST; Q13705; -.
DR   MassIVE; Q13705; -.
DR   PaxDb; 9606-ENSP00000340361; -.
DR   PeptideAtlas; Q13705; -.
DR   ProteomicsDB; 59666; -. [Q13705-1]
DR   Pumba; Q13705; -.
DR   ABCD; Q13705; 1 sequenced antibody.
DR   Antibodypedia; 12076; 520 antibodies from 33 providers.
DR   DNASU; 93; -.
DR   Ensembl; ENST00000352511.5; ENSP00000340361.3; ENSG00000114739.14. [Q13705-1]
DR   GeneID; 93; -.
DR   KEGG; hsa:93; -.
DR   MANE-Select; ENST00000352511.5; ENSP00000340361.3; NM_001106.4; NP_001097.2.
DR   UCSC; uc003cif.4; human. [Q13705-1]
DR   AGR; HGNC:174; -.
DR   CTD; 93; -.
DR   DisGeNET; 93; -.
DR   GeneCards; ACVR2B; -.
DR   HGNC; HGNC:174; ACVR2B.
DR   HPA; ENSG00000114739; Low tissue specificity.
DR   MalaCards; ACVR2B; -.
DR   MIM; 602730; gene.
DR   MIM; 613751; phenotype.
DR   neXtProt; NX_Q13705; -.
DR   OpenTargets; ENSG00000114739; -.
DR   Orphanet; 157769; Situs ambiguus.
DR   PharmGKB; PA24495; -.
DR   VEuPathDB; HostDB:ENSG00000114739; -.
DR   eggNOG; KOG3653; Eukaryota.
DR   GeneTree; ENSGT00940000156210; -.
DR   HOGENOM; CLU_000288_8_4_1; -.
DR   InParanoid; Q13705; -.
DR   OMA; SWNDLCH; -.
DR   OrthoDB; 3900892at2759; -.
DR   PhylomeDB; Q13705; -.
DR   TreeFam; TF352876; -.
DR   PathwayCommons; Q13705; -.
DR   Reactome; R-HSA-1181150; Signaling by NODAL.
DR   Reactome; R-HSA-1433617; Regulation of signaling by NODAL.
DR   Reactome; R-HSA-1502540; Signaling by Activin.
DR   Reactome; R-HSA-201451; Signaling by BMP.
DR   SignaLink; Q13705; -.
DR   SIGNOR; Q13705; -.
DR   BioGRID-ORCS; 93; 19 hits in 1164 CRISPR screens.
DR   ChiTaRS; ACVR2B; human.
DR   EvolutionaryTrace; Q13705; -.
DR   GeneWiki; ACVR2B; -.
DR   GenomeRNAi; 93; -.
DR   Pharos; Q13705; Tchem.
DR   PRO; PR:Q13705; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q13705; Protein.
DR   Bgee; ENSG00000114739; Expressed in secondary oocyte and 186 other cell types or tissues.
DR   Genevisible; Q13705; HS.
DR   GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR   GO; GO:0043235; C:receptor complex; IPI:BHF-UCL.
DR   GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR   GO; GO:0017002; F:activin receptor activity; IBA:GO_Central.
DR   GO; GO:0016362; F:activin receptor activity, type II; IDA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019838; F:growth factor binding; IPI:HGNC-UCL.
DR   GO; GO:0019209; F:kinase activator activity; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:HGNC-UCL.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:Ensembl.
DR   GO; GO:0032924; P:activin receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:HGNC-UCL.
DR   GO; GO:0060840; P:artery development; ISS:BHF-UCL.
DR   GO; GO:0001974; P:blood vessel remodeling; ISS:BHF-UCL.
DR   GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR   GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR   GO; GO:0048617; P:embryonic foregut morphogenesis; IEA:Ensembl.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0001946; P:lymphangiogenesis; ISS:BHF-UCL.
DR   GO; GO:0060836; P:lymphatic endothelial cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0007498; P:mesoderm development; IEA:Ensembl.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:BHF-UCL.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0035265; P:organ growth; IEA:Ensembl.
DR   GO; GO:0031016; P:pancreas development; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IDA:HGNC-UCL.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; IMP:BHF-UCL.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:HGNC-UCL.
DR   GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR   GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:BHF-UCL.
DR   GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IDA:HGNC-UCL.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR   GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; TAS:ProtInc.
DR   GO; GO:0060841; P:venous blood vessel development; ISS:BHF-UCL.
DR   CDD; cd14140; STKc_ACVR2b; 1.
DR   Gene3D; 2.10.60.10; CD59; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000472; Activin_recp.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255:SF70; ACTIVIN RECEPTOR TYPE-2B; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF57302; Snake toxin-like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW   Disease variant; Disulfide bond; Glycoprotein; Heterotaxy; Kinase;
KW   Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Receptor; Reference proteome;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..512
FT                   /note="Activin receptor type-2B"
FT                   /id="PRO_0000024404"
FT   TOPO_DOM        19..137
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..512
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          190..480
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          491..512
FT                   /note="Interaction with DYNLT1"
FT                   /evidence="ECO:0000250|UniProtKB:P27040"
FT   ACT_SITE        321
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         196..204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22718755"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22718755"
FT   DISULFID        29..59
FT                   /evidence="ECO:0000269|PubMed:22718755"
FT   DISULFID        49..77
FT                   /evidence="ECO:0000269|PubMed:22718755"
FT   DISULFID        84..103
FT                   /evidence="ECO:0000269|PubMed:22718755"
FT   DISULFID        90..102
FT                   /evidence="ECO:0000269|PubMed:22718755"
FT   DISULFID        104..109
FT                   /evidence="ECO:0000269|PubMed:22718755"
FT   VARIANT         40
FT                   /note="R -> H (in HTX4; dbSNP:rs121434437)"
FT                   /evidence="ECO:0000269|PubMed:9916847"
FT                   /id="VAR_013281"
FT   VARIANT         176
FT                   /note="P -> R (in dbSNP:rs35882617)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041396"
FT   VARIANT         459
FT                   /note="E -> D (in dbSNP:rs500611)"
FT                   /evidence="ECO:0000269|PubMed:9621519"
FT                   /id="VAR_050594"
FT   VARIANT         494
FT                   /note="V -> I (in HTX4; dbSNP:rs121434438)"
FT                   /evidence="ECO:0000269|PubMed:9916847"
FT                   /id="VAR_013282"
FT   CONFLICT        16..17
FT                   /note="CA -> WP (in Ref. 1; CAA54671)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        64
FT                   /note="R -> A (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        459
FT                   /note="E -> A (in Ref. 3; AAC64515)"
FT                   /evidence="ECO:0000305"
FT   STRAND          27..33
FT                   /evidence="ECO:0007829|PDB:2H62"
FT   HELIX           36..39
FT                   /evidence="ECO:0007829|PDB:2H62"
FT   STRAND          43..49
FT                   /evidence="ECO:0007829|PDB:2H62"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:5NGV"
FT   STRAND          57..66
FT                   /evidence="ECO:0007829|PDB:2H62"
FT   STRAND          69..79
FT                   /evidence="ECO:0007829|PDB:2H62"
FT   HELIX           82..84
FT                   /evidence="ECO:0007829|PDB:2H62"
FT   STRAND          88..91
FT                   /evidence="ECO:0007829|PDB:2H62"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:5NGV"
FT   STRAND          98..106
FT                   /evidence="ECO:0007829|PDB:2H62"
FT   TURN            107..110
FT                   /evidence="ECO:0007829|PDB:2H62"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:2H62"
FT   STRAND          191..197
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   STRAND          200..209
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   STRAND          212..219
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   HELIX           221..223
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   HELIX           224..235
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   STRAND          247..253
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   TURN            256..258
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   STRAND          260..266
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   HELIX           273..279
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   HELIX           284..302
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   STRAND          305..308
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   TURN            309..311
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   STRAND          312..314
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   STRAND          316..318
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   HELIX           324..326
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   STRAND          327..329
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   STRAND          335..337
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   STRAND          344..346
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   HELIX           362..364
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   HELIX           367..370
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   HELIX           378..398
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   TURN            413..417
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   HELIX           424..431
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   HELIX           442..446
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   HELIX           448..460
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   HELIX           465..467
FT                   /evidence="ECO:0007829|PDB:2QLU"
FT   HELIX           471..482
FT                   /evidence="ECO:0007829|PDB:2QLU"
SQ   SEQUENCE   512 AA;  57724 MW;  B377FEF92EF74937 CRC64;
     MTAPWVALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GEQDKRLHCY
     ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEAG
     GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP
     PSPLVGLKPL QLLEIKARGR FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK
     HENLLQFIAA EKRGSNLEVE LWLITAFHDK GSLTDYLKGN IITWNELCHV AETMSRGLSY
     LHEDVPWCRG EGHKPSIAHR DFKSKNVLLK SDLTAVLADF GLAVRFEPGK PPGDTHGQVG
     TRRYMAPEVL EGAINFQRDA FLRIDMYAMG LVLWELVSRC KAADGPVDEY MLPFEEEIGQ
     HPSLEELQEV VVHKKMRPTI KDHWLKHPGL AQLCVTIEEC WDHDAEARLS AGCVEERVSL
     IRRSVNGTTS DCLVSLVTSV TNVDLPPKES SI
//
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