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Entry version 197 (13 Feb 2019)
Sequence version 3 (16 May 2006)
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Protein

Activin receptor type-2B

Gene

ACVR2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei217ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei321Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi196 – 204ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Receptor, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1181150 Signaling by NODAL
R-HSA-1433617 Regulation of signaling by NODAL
R-HSA-1502540 Signaling by Activin
R-HSA-201451 Signaling by BMP

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q13705

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q13705

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Activin receptor type-2B (EC:2.7.11.30)
Alternative name(s):
Activin receptor type IIB
Short name:
ACTR-IIB
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ACVR2B
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000114739.13

Human Gene Nomenclature Database

More...
HGNCi
HGNC:174 ACVR2B

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
602730 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q13705

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini19 – 137ExtracellularSequence analysisAdd BLAST119
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei138 – 158HelicalSequence analysisAdd BLAST21
Topological domaini159 – 512CytoplasmicSequence analysisAdd BLAST354

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Heterotaxy, visceral, 4, autosomal (HTX4)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of visceral heterotaxy, a complex disorder due to disruption of the normal left-right asymmetry of the thoracoabdominal organs. Visceral heterotaxy or situs ambiguus results in randomization of the placement of visceral organs, including the heart, lungs, liver, spleen, and stomach. The organs are oriented randomly with respect to the left-right axis and with respect to one another. It can been associated with variety of congenital defects including cardiac malformations. HTX4 clinical features include dextrocardia, right aortic arch and a right-sided spleen, anomalies of the inferior and the superior vena cava, atrial ventricular canal defect with dextro-transposed great arteries, pulmonary stenosis, polysplenia and midline liver.
See also OMIM:613751
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01328140R → H in HTX4. 1 PublicationCorresponds to variant dbSNP:rs121434437EnsemblClinVar.1
Natural variantiVAR_013282494V → I in HTX4. 1 PublicationCorresponds to variant dbSNP:rs121434438EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Heterotaxy

Organism-specific databases

DisGeNET

More...
DisGeNETi
93

MalaCards human disease database

More...
MalaCardsi
ACVR2B
MIMi613751 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000114739

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
157769 Situs ambiguus

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA24495

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5466

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1792

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ACVR2B

Domain mapping of disease mutations (DMDM)

More...
DMDMi
97535735

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 18Sequence analysisAdd BLAST18
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002440419 – 512Activin receptor type-2BAdd BLAST494

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi29 ↔ 591 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi42N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi49 ↔ 771 Publication
Glycosylationi65N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi84 ↔ 1031 Publication
Disulfide bondi90 ↔ 1021 Publication
Disulfide bondi104 ↔ 1091 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated. Constitutive phosphorylation is in part catalyzed by its own kinase activity.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q13705

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q13705

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q13705

PeptideAtlas

More...
PeptideAtlasi
Q13705

PRoteomics IDEntifications database

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PRIDEi
Q13705

ProteomicsDB human proteome resource

More...
ProteomicsDBi
59666

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q13705

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q13705

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000114739 Expressed in 210 organ(s), highest expression level in secondary oocyte

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q13705 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB025115
HPA007398
HPA040384

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms an activin receptor complex with activin type II receptors such as ACVR1B. Interacts with VPS39. Interacts with DYNLT1.By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
MSTNO147934EBI-1383577,EBI-8542977

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
106608, 77 interactors

Protein interaction database and analysis system

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IntActi
Q13705, 6 interactors

Molecular INTeraction database

More...
MINTi
Q13705

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000340361

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q13705

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H62X-ray1.85D19-116[»]
2QLUX-ray2.00A190-487[»]
4FAOX-ray3.36E/F/K/L/Q/R/W/X/e/f/k/l19-134[»]
5NGVX-ray2.00A24-117[»]
5NHRX-ray3.35C/D24-117[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q13705

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q13705

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q13705

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini190 – 480Protein kinasePROSITE-ProRule annotationAdd BLAST291

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni491 – 512Interaction with DYNLT1By similarityAdd BLAST22

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3653 Eukaryota
ENOG410XS2Z LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156210

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG054502

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q13705

KEGG Orthology (KO)

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KOi
K13596

Identification of Orthologs from Complete Genome Data

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OMAi
PAIKDHW

Database of Orthologous Groups

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OrthoDBi
390511at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q13705

TreeFam database of animal gene trees

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TreeFami
TF352876

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000472 Activin_recp
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS
IPR000333 TGFB_receptor

The PANTHER Classification System

More...
PANTHERi
PTHR23255 PTHR23255, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01064 Activin_recp, 1 hit
PF00069 Pkinase, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00653 ACTIVIN2R

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform ActR-IIB2 (identifier: Q13705-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MTAPWVALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE
60 70 80 90 100
GEQDKRLHCY ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY
110 120 130 140 150
FCCCEGNFCN ERFTHLPEAG GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS
160 170 180 190 200
LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP PSPLVGLKPL QLLEIKARGR
210 220 230 240 250
FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK HENLLQFIAA
260 270 280 290 300
EKRGSNLEVE LWLITAFHDK GSLTDYLKGN IITWNELCHV AETMSRGLSY
310 320 330 340 350
LHEDVPWCRG EGHKPSIAHR DFKSKNVLLK SDLTAVLADF GLAVRFEPGK
360 370 380 390 400
PPGDTHGQVG TRRYMAPEVL EGAINFQRDA FLRIDMYAMG LVLWELVSRC
410 420 430 440 450
KAADGPVDEY MLPFEEEIGQ HPSLEELQEV VVHKKMRPTI KDHWLKHPGL
460 470 480 490 500
AQLCVTIEEC WDHDAEARLS AGCVEERVSL IRRSVNGTTS DCLVSLVTSV
510
TNVDLPPKES SI
Length:512
Mass (Da):57,724
Last modified:May 16, 2006 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB377FEF92EF74937
GO
Isoform ActR-IIB1 (identifier: Q13705-2)
Sequence is not available
Note: Produced from the insertion in the transcript of 82 base pairs, leading to frameshift and protein truncation. May be not functional.
Length:
Mass (Da):

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti16 – 17CA → WP in CAA54671 (PubMed:8161782).Curated2
Sequence conflicti64R → A (PubMed:8161782).Curated1
Sequence conflicti64R → A (PubMed:9621519).Curated1
Sequence conflicti459E → A in AAC64515 (PubMed:9916847).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01328140R → H in HTX4. 1 PublicationCorresponds to variant dbSNP:rs121434437EnsemblClinVar.1
Natural variantiVAR_041396176P → R1 PublicationCorresponds to variant dbSNP:rs35882617Ensembl.1
Natural variantiVAR_050594459E → D1 PublicationCorresponds to variant dbSNP:rs500611Ensembl.1
Natural variantiVAR_013282494V → I in HTX4. 1 PublicationCorresponds to variant dbSNP:rs121434438EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X77533 mRNA Translation: CAA54671.1
AB008681 Genomic DNA Translation: BAA24180.2
AF060202
, AF060199, AF060200, AF060201 Genomic DNA Translation: AAC64515.1
BC096243 mRNA Translation: AAH96243.1
BC096244 mRNA Translation: AAH96244.1
BC099642 mRNA Translation: AAH99642.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS2679.1 [Q13705-1]

Protein sequence database of the Protein Information Resource

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PIRi
I37134

NCBI Reference Sequences

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RefSeqi
NP_001097.2, NM_001106.3 [Q13705-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.174273

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000352511; ENSP00000340361; ENSG00000114739 [Q13705-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
93

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:93

UCSC genome browser

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UCSCi
uc003cif.4 human [Q13705-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77533 mRNA Translation: CAA54671.1
AB008681 Genomic DNA Translation: BAA24180.2
AF060202
, AF060199, AF060200, AF060201 Genomic DNA Translation: AAC64515.1
BC096243 mRNA Translation: AAH96243.1
BC096244 mRNA Translation: AAH96244.1
BC099642 mRNA Translation: AAH99642.1
CCDSiCCDS2679.1 [Q13705-1]
PIRiI37134
RefSeqiNP_001097.2, NM_001106.3 [Q13705-1]
UniGeneiHs.174273

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H62X-ray1.85D19-116[»]
2QLUX-ray2.00A190-487[»]
4FAOX-ray3.36E/F/K/L/Q/R/W/X/e/f/k/l19-134[»]
5NGVX-ray2.00A24-117[»]
5NHRX-ray3.35C/D24-117[»]
ProteinModelPortaliQ13705
SMRiQ13705
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106608, 77 interactors
IntActiQ13705, 6 interactors
MINTiQ13705
STRINGi9606.ENSP00000340361

Chemistry databases

BindingDBiQ13705
ChEMBLiCHEMBL5466
GuidetoPHARMACOLOGYi1792

PTM databases

iPTMnetiQ13705
PhosphoSitePlusiQ13705

Polymorphism and mutation databases

BioMutaiACVR2B
DMDMi97535735

Proteomic databases

EPDiQ13705
jPOSTiQ13705
PaxDbiQ13705
PeptideAtlasiQ13705
PRIDEiQ13705
ProteomicsDBi59666

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
93
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000352511; ENSP00000340361; ENSG00000114739 [Q13705-1]
GeneIDi93
KEGGihsa:93
UCSCiuc003cif.4 human [Q13705-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
93
DisGeNETi93
EuPathDBiHostDB:ENSG00000114739.13

GeneCards: human genes, protein and diseases

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GeneCardsi
ACVR2B
HGNCiHGNC:174 ACVR2B
HPAiCAB025115
HPA007398
HPA040384
MalaCardsiACVR2B
MIMi602730 gene
613751 phenotype
neXtProtiNX_Q13705
OpenTargetsiENSG00000114739
Orphaneti157769 Situs ambiguus
PharmGKBiPA24495

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3653 Eukaryota
ENOG410XS2Z LUCA
GeneTreeiENSGT00940000156210
HOVERGENiHBG054502
InParanoidiQ13705
KOiK13596
OMAiPAIKDHW
OrthoDBi390511at2759
PhylomeDBiQ13705
TreeFamiTF352876

Enzyme and pathway databases

ReactomeiR-HSA-1181150 Signaling by NODAL
R-HSA-1433617 Regulation of signaling by NODAL
R-HSA-1502540 Signaling by Activin
R-HSA-201451 Signaling by BMP
SignaLinkiQ13705
SIGNORiQ13705

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
ACVR2B human
EvolutionaryTraceiQ13705

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
ACVR2B

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
93

Protein Ontology

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PROi
PR:Q13705

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000114739 Expressed in 210 organ(s), highest expression level in secondary oocyte
GenevisibleiQ13705 HS

Family and domain databases

InterProiView protein in InterPro
IPR000472 Activin_recp
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS
IPR000333 TGFB_receptor
PANTHERiPTHR23255 PTHR23255, 1 hit
PfamiView protein in Pfam
PF01064 Activin_recp, 1 hit
PF00069 Pkinase, 1 hit
PRINTSiPR00653 ACTIVIN2R
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAVR2B_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q13705
Secondary accession number(s): Q4VAV0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 16, 2006
Last modified: February 13, 2019
This is version 197 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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