ACVR1B
entrez
91
canonical
uniprot
P36896
canonical
ensembl
ENSG00000135503
resolver
ensp
ENSP00000257963
resolver
ensp
ENSP00000442656
resolver
ensp
ENSP00000442885
resolver
ensp
ENSP00000570404
resolver
ensp
ENSP00000570405
resolver
ensp
ENSP00000570406
resolver
ensp
ENSP00000570408
resolver
ensp
ENSP00000570409
resolver
ensp
ENSP00000586315
resolver
ensp
ENSP00000664179
resolver
genesymbol
ACVR1B
resolver
genesymbol_syn
ACVRLK4
resolver
genesymbol_syn
ALK4
resolver
hgnc
HGNC:172
resolver
uniprot
B7Z5L8
resolver
uniprot
B7Z5W5
resolver
uniprot
Q15479
resolver
uniprot
Q15480
resolver
uniprot
Q15481
resolver
uniprot
Q15482
resolver
uniprot_entry
ACV1B_HUMAN
resolver
uniprot_sec
B7Z5L8
resolver
uniprot_sec
B7Z5W5
resolver
uniprot_sec
Q15479
resolver
uniprot_sec
Q15480
resolver
uniprot_sec
Q15481
resolver
uniprot_sec
Q15482
resolver
activity_regulation
ACTIVITY REGULATION: Activin receptor type-2 (ACVR2A or ACVR2B) activates the type-1 receptor through phosphorylation of its regulatory GS domain. {ECO:0000269|PubMed:11266516, ECO:0000269|PubMed:11909953}.
uniprot
proteins
amino_acid_sequence
MAESAGASSFFPLVVLLLAGSGGSGPRGVQALLCACTSCLQANYTCETDGACMVSIFNLDGMEHHVRTCIPKVELVPAGKPFYCLSSEDLRNTHCCYTDYCNRIDLRVPSGHLKEPEHPSMWGPVELVGIIAGPVFLLFLIIIIVFLVINYHQRVYHNRQRLDMEDPSCEMCLSKDKTLQDLVYDLSTSGSGSGLPLFVQRTVARTIVLQEIIGKGRFGEVWRGRWRGGDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTIEGMIKLALSAASGLAHLHMEIVGTQGKPGIAHRDLKSKNILVKKNGMCAIADLGLAVRHDAVTDTIDIAPNQRVGTKRYMAPEVLDETINMKHFDSFKCADIYALGLVYWEIARRCNSGGVHEEYQLPYYDLVPSDPSIEEMRKVVCDQKLRPNIPNWWQSYEALRVMGKMMRECWYANGAARLTALRIKKTLSQLSVQEDVKI
uniprot
proteins
disease_involvement
DISEASE: Note=ACVRIB is abundantly expressed in systemic sclerosis patient fibroblasts and production of collagen is also induced by activin-A/INHBA. This suggests that the activin/ACRV1B signaling mechanism is involved in systemic sclerosis. {ECO:0000269|PubMed:21377836}.
uniprot
proteins
ec_number
2.7.11.30
uniprot
proteins
function
FUNCTION: Transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a 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, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas 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 such as ACVR1B. 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. ACVR1B also phosphorylates TDP2. {ECO:0000269|PubMed:12364468, ECO:0000269|PubMed:12639945, ECO:0000269|PubMed:18039968, ECO:0000269|PubMed:20226172, ECO:0000269|PubMed:8196624, ECO:0000269|PubMed:9032295, ECO:0000269|PubMed:9892009}.
uniprot
proteins
mass_dalton
56807
uniprot
proteins
mutagenesis
MUTAGEN 40; /note="L->A: Increases binding to activin."; /evidence="ECO:0000269|PubMed:12665502"; MUTAGEN 70; /note="I->A: Decreases binding to activin."; /evidence="ECO:0000269|PubMed:12665502"; MUTAGEN 73; /note="V->A: Increases binding to activin."; /evidence="ECO:0000269|PubMed:12665502"; MUTAGEN 75; /note="L->A: Decreases binding to activin."; /evidence="ECO:0000269|PubMed:12665502"; MUTAGEN 77; /note="P->A: Decreases binding to activin."; /evidence="ECO:0000269|PubMed:12665502"; MUTAGEN 206; /note="T->V: Leads to constitutive activation."; /evidence="ECO:0000269|PubMed:8622651
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated. Phosphorylated by activin receptor type-2 (ACVR2A or ACVR2B) in response to activin-binding at serine and threonine residues in the GS domain. Phosphorylation of ACVR1B by activin receptor type-2 regulates association with SMAD7. {ECO:0000269|PubMed:12023024, ECO:0000269|PubMed:12112843, ECO:0000269|PubMed:12364468, ECO:0000269|PubMed:8622651}.; PTM: Ubiquitinated. Level of ubiquitination is regulated by the SMAD7-SMURF1 complex.; PTM: Ubiquitinated.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
TGFB receptor subfamily
uniprot
proteins
protein_family
TKL Ser/Thr protein kinase family
uniprot
proteins
pubmed
11266516
uniprot
proteins
pubmed
11909953
uniprot
proteins
pubmed
12023024
uniprot
proteins
pubmed
12112843
uniprot
proteins
pubmed
12364468
uniprot
proteins
pubmed
12639945
uniprot
proteins
pubmed
12665502
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16720724
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18039968
uniprot
proteins
pubmed
20226172
uniprot
proteins
pubmed
20596523
uniprot
proteins
pubmed
21377836
uniprot
proteins
pubmed
21791611
uniprot
proteins
pubmed
8058741
uniprot
proteins
pubmed
8196624
uniprot
proteins
pubmed
8397373
uniprot
proteins
pubmed
8622651
uniprot
proteins
pubmed
9032295
uniprot
proteins
pubmed
9892009
uniprot
proteins
sequence_length
505
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 127..149; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins