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Protein

Activin receptor type-1B

Gene

ACVR1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 TDP2.7 Publications

Catalytic activityi

ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.

Cofactori

Mg2+By similarity, Mn2+By similarity

Enzyme regulationi

Activin receptor type-2 (ACVR2A or ACVR2B) activates the type-1 receptor through phosphorylation of its regulatory GS domain.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei234 – 2341ATPPROSITE-ProRule annotation
Active sitei335 – 3351Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi213 – 2219ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • activin receptor activity, type I Source: UniProtKB
  • ATP binding Source: HGNC
  • inhibin binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: UniProtKB
  • receptor signaling protein serine/threonine kinase activity Source: Ensembl
  • SMAD binding Source: HGNC
  • transmembrane receptor protein serine/threonine kinase activity Source: HGNC
  • ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

  • activin receptor signaling pathway Source: UniProtKB
  • central nervous system development Source: Ensembl
  • development of primary female sexual characteristics Source: Ensembl
  • extrinsic apoptotic signaling pathway Source: BHF-UCL
  • G1/S transition of mitotic cell cycle Source: HGNC
  • hair follicle development Source: Ensembl
  • in utero embryonic development Source: Ensembl
  • negative regulation of cell growth Source: HGNC
  • negative regulation of gene expression Source: Ensembl
  • nodal signaling pathway Source: UniProtKB
  • peptidyl-threonine phosphorylation Source: UniProtKB
  • positive regulation of activin receptor signaling pathway Source: BHF-UCL
  • positive regulation of erythrocyte differentiation Source: HGNC
  • positive regulation of pathway-restricted SMAD protein phosphorylation Source: Ensembl
  • positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • positive regulation of trophoblast cell migration Source: BHF-UCL
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: HGNC
  • regulation of transcription, DNA-templated Source: HGNC
  • signal transduction Source: HGNC
  • transmembrane receptor protein serine/threonine kinase signaling pathway Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_111057. Signaling by NODAL.
REACT_111059. Regulation of signaling by NODAL.
REACT_150238. Signaling by Activin.
SignaLinkiP36896.

Names & Taxonomyi

Protein namesi
Recommended name:
Activin receptor type-1B (EC:2.7.11.30)
Alternative name(s):
Activin receptor type IB
Short name:
ACTR-IB
Activin receptor-like kinase 4
Short name:
ALK-4
Serine/threonine-protein kinase receptor R2
Short name:
SKR2
Gene namesi
Name:ACVR1B
Synonyms:ACVRLK4, ALK4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:172. ACVR1B.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 126103ExtracellularSequence AnalysisAdd
BLAST
Transmembranei127 – 14923HelicalSequence AnalysisAdd
BLAST
Topological domaini150 – 505356CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • activin receptor complex Source: BHF-UCL
  • cell surface Source: HGNC
  • extracellular exosome Source: UniProtKB
  • integral component of plasma membrane Source: HGNC
  • plasma membrane Source: Reactome
  • receptor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401L → A: Increases binding to activin. 1 Publication
Mutagenesisi70 – 701I → A: Decreases binding to activin. 1 Publication
Mutagenesisi73 – 731V → A: Increases binding to activin. 1 Publication
Mutagenesisi75 – 751L → A: Decreases binding to activin. 1 Publication
Mutagenesisi77 – 771P → A: Decreases binding to activin. 1 Publication
Mutagenesisi206 – 2061T → V: Leads to constitutive activation. 1 Publication

Organism-specific databases

PharmGKBiPA24493.

Chemistry

DrugBankiDB00171. Adenosine triphosphate.

Polymorphism and mutation databases

BioMutaiACVR1B.
DMDMi547775.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 505482Activin receptor type-1BPRO_0000024417Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...)Sequence Analysis
Modified residuei380 – 3801Phosphotyrosine1 Publication

Post-translational modificationi

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 SMAD7.4 Publications
Ubiquitinated. Level of ubiquitination is regulated by the SMAD7-SMURF1 complex.
Ubiquitinated.

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP36896.
PaxDbiP36896.
PRIDEiP36896.

PTM databases

PhosphoSiteiP36896.

Expressioni

Tissue specificityi

Expressed in many tissues, most strongly in kidney, pancreas, brain, lung, and liver.

Gene expression databases

BgeeiP36896.
CleanExiHS_ACVR1B.
ExpressionAtlasiP36896. baseline and differential.
GenevisibleiP36896. HS.

Organism-specific databases

HPAiCAB026126.
HPA063761.

Interactioni

Subunit structurei

Forms an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Interacts with TDP2 (By similarity). Interacts with AIP1, FKBP1A, IGSF1, TDGF1, SMAD2, SMAD3 and SMAD7.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FKBP1AP629422EBI-1384128,EBI-1027571
HSP90AB1P082382EBI-1384128,EBI-352572
SMAD7O151052EBI-1384128,EBI-3861591

Protein-protein interaction databases

BioGridi106606. 32 interactions.
DIPiDIP-427N.
IntActiP36896. 8 interactions.
STRINGi9606.ENSP00000442656.

Structurei

3D structure databases

ProteinModelPortaliP36896.
SMRiP36896. Positions 31-104, 149-501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini177 – 20630GSPROSITE-ProRule annotationAdd
BLAST
Domaini207 – 497291Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

The GS domain is a 30-amino-acid sequence adjacent to the N-terminal boundary of the kinase domain and highly conserved in all other known type-1 receptors but not in type-2 receptors. The GS domain is the site of activation through phosphorylation by the II receptors.1 Publication

Sequence similaritiesi

Contains 1 GS domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118876.
HOGENOMiHOG000230587.
HOVERGENiHBG054502.
InParanoidiP36896.
KOiK13567.
OMAiNTHCCYE.
OrthoDBiEOG7Q8CN3.
PhylomeDBiP36896.
TreeFamiTF314724.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR000472. TFB_recept_I/II_C.
IPR003605. TGF_beta_rcpt_GS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PfamiPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
SMARTiSM00467. GS. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P36896-1) [UniParc]FASTAAdd to basket

Also known as: SKR2-1

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.

« Hide

        10         20         30         40         50
MAESAGASSF FPLVVLLLAG SGGSGPRGVQ ALLCACTSCL QANYTCETDG
60 70 80 90 100
ACMVSIFNLD GMEHHVRTCI PKVELVPAGK PFYCLSSEDL RNTHCCYTDY
110 120 130 140 150
CNRIDLRVPS GHLKEPEHPS MWGPVELVGI IAGPVFLLFL IIIIVFLVIN
160 170 180 190 200
YHQRVYHNRQ RLDMEDPSCE MCLSKDKTLQ DLVYDLSTSG SGSGLPLFVQ
210 220 230 240 250
RTVARTIVLQ EIIGKGRFGE VWRGRWRGGD VAVKIFSSRE ERSWFREAEI
260 270 280 290 300
YQTVMLRHEN ILGFIAADNK DNGTWTQLWL VSDYHEHGSL FDYLNRYTVT
310 320 330 340 350
IEGMIKLALS AASGLAHLHM EIVGTQGKPG IAHRDLKSKN ILVKKNGMCA
360 370 380 390 400
IADLGLAVRH DAVTDTIDIA PNQRVGTKRY MAPEVLDETI NMKHFDSFKC
410 420 430 440 450
ADIYALGLVY WEIARRCNSG GVHEEYQLPY YDLVPSDPSI EEMRKVVCDQ
460 470 480 490 500
KLRPNIPNWW QSYEALRVMG KMMRECWYAN GAARLTALRI KKTLSQLSVQ

EDVKI
Length:505
Mass (Da):56,807
Last modified:June 1, 1994 - v1
Checksum:i40A6C65CAA4C7573
GO
Isoform 2 (identifier: P36896-2) [UniParc]FASTAAdd to basket

Also known as: SKR2-2

The sequence of this isoform differs from the canonical sequence as follows:
     465-505: ALRVMGKMMRECWYANGAARLTALRIKKTLSQLSVQEDVKI → VRSWPPAAFPSA

Show »
Length:476
Mass (Da):53,411
Checksum:i13269BD6D04F39D3
GO
Isoform 3 (identifier: P36896-3) [UniParc]FASTAAdd to basket

Also known as: SKR2-3

The sequence of this isoform differs from the canonical sequence as follows:
     422-505: VHEEYQLPYY...QLSVQEDVKI → TFLFCLCSYL...RLFFRDQFVE

Show »
Length:487
Mass (Da):54,270
Checksum:i969525A044E8F7C6
GO
Isoform 4 (identifier: P36896-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     271-271: D → ADCSFLTLPWEVVMVSAAPKLRSLRLQYKGGRGRARFLFPLN

Show »
Length:546
Mass (Da):61,439
Checksum:i0A75C7D6FE406EB3
GO
Isoform 5 (identifier: P36896-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.

Show »
Length:453
Mass (Da):51,725
Checksum:i8E6885B168A1B026
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561I → F in AAA60555 (PubMed:8058741).Curated
Sequence conflicti56 – 561I → F in AAA60556 (PubMed:8058741).Curated
Sequence conflicti222 – 2232WR → MA in AAA60555 (PubMed:8058741).Curated
Sequence conflicti222 – 2232WR → MA in AAA60556 (PubMed:8058741).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti146 – 1461F → L.1 Publication
Corresponds to variant rs34488074 [ dbSNP | Ensembl ].
VAR_041406
Natural varianti408 – 4081L → V.
Corresponds to variant rs928906 [ dbSNP | Ensembl ].
VAR_011716
Isoform 3 (identifier: P36896-3)
Natural varianti478 – 4781R → H.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5252Missing in isoform 5. 1 PublicationVSP_041841Add
BLAST
Alternative sequencei271 – 2711D → ADCSFLTLPWEVVMVSAAPK LRSLRLQYKGGRGRARFLFP LN in isoform 4. 1 PublicationVSP_041842
Alternative sequencei422 – 50584VHEEY…EDVKI → TFLFCLCSYLPFQDAGSPKA VLLPPFFLQPVGCLLPEPES SFKVAIKGVEVAVLRVRLFF RDQFVE in isoform 3. 1 PublicationVSP_004953Add
BLAST
Alternative sequencei465 – 50541ALRVM…EDVKI → VRSWPPAAFPSA in isoform 2. 1 PublicationVSP_004954Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22536 mRNA. Translation: CAA80258.1.
U14722 mRNA. Translation: AAA50246.1.
L10125 mRNA. Translation: AAA60555.1.
L10126 mRNA. Translation: AAA60556.1.
L31848 Genomic DNA. Translation: AAA53349.1.
L31848 Genomic DNA. Translation: AAA53350.1.
L31848 Genomic DNA. Translation: AAA53351.1.
BT007072 mRNA. Translation: AAP35735.1.
AK299120 mRNA. Translation: BAH12954.1.
AK299496 mRNA. Translation: BAH13051.1.
AC025259 Genomic DNA. No translation available.
BC000254 mRNA. Translation: AAH00254.1.
BC040531 mRNA. Translation: AAH40531.1.
CCDSiCCDS44893.2. [P36896-5]
CCDS44894.2. [P36896-4]
CCDS8816.1. [P36896-1]
PIRiI38859.
I80182.
I80183.
RefSeqiNP_004293.1. NM_004302.4. [P36896-1]
NP_064732.3. NM_020327.3. [P36896-5]
NP_064733.3. NM_020328.3. [P36896-4]
UniGeneiHs.438918.

Genome annotation databases

EnsembliENST00000257963; ENSP00000257963; ENSG00000135503. [P36896-1]
ENST00000415850; ENSP00000397550; ENSG00000135503. [P36896-3]
ENST00000426655; ENSP00000390477; ENSG00000135503. [P36896-2]
ENST00000541224; ENSP00000442656; ENSG00000135503. [P36896-4]
ENST00000542485; ENSP00000442885; ENSG00000135503. [P36896-5]
GeneIDi91.
KEGGihsa:91.
UCSCiuc001rzl.3. human. [P36896-3]
uc001rzm.3. human. [P36896-2]
uc001rzn.3. human. [P36896-1]
uc010snn.2. human. [P36896-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22536 mRNA. Translation: CAA80258.1.
U14722 mRNA. Translation: AAA50246.1.
L10125 mRNA. Translation: AAA60555.1.
L10126 mRNA. Translation: AAA60556.1.
L31848 Genomic DNA. Translation: AAA53349.1.
L31848 Genomic DNA. Translation: AAA53350.1.
L31848 Genomic DNA. Translation: AAA53351.1.
BT007072 mRNA. Translation: AAP35735.1.
AK299120 mRNA. Translation: BAH12954.1.
AK299496 mRNA. Translation: BAH13051.1.
AC025259 Genomic DNA. No translation available.
BC000254 mRNA. Translation: AAH00254.1.
BC040531 mRNA. Translation: AAH40531.1.
CCDSiCCDS44893.2. [P36896-5]
CCDS44894.2. [P36896-4]
CCDS8816.1. [P36896-1]
PIRiI38859.
I80182.
I80183.
RefSeqiNP_004293.1. NM_004302.4. [P36896-1]
NP_064732.3. NM_020327.3. [P36896-5]
NP_064733.3. NM_020328.3. [P36896-4]
UniGeneiHs.438918.

3D structure databases

ProteinModelPortaliP36896.
SMRiP36896. Positions 31-104, 149-501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106606. 32 interactions.
DIPiDIP-427N.
IntActiP36896. 8 interactions.
STRINGi9606.ENSP00000442656.

Chemistry

BindingDBiP36896.
ChEMBLiCHEMBL5310.
DrugBankiDB00171. Adenosine triphosphate.
GuidetoPHARMACOLOGYi1787.

PTM databases

PhosphoSiteiP36896.

Polymorphism and mutation databases

BioMutaiACVR1B.
DMDMi547775.

Proteomic databases

MaxQBiP36896.
PaxDbiP36896.
PRIDEiP36896.

Protocols and materials databases

DNASUi91.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257963; ENSP00000257963; ENSG00000135503. [P36896-1]
ENST00000415850; ENSP00000397550; ENSG00000135503. [P36896-3]
ENST00000426655; ENSP00000390477; ENSG00000135503. [P36896-2]
ENST00000541224; ENSP00000442656; ENSG00000135503. [P36896-4]
ENST00000542485; ENSP00000442885; ENSG00000135503. [P36896-5]
GeneIDi91.
KEGGihsa:91.
UCSCiuc001rzl.3. human. [P36896-3]
uc001rzm.3. human. [P36896-2]
uc001rzn.3. human. [P36896-1]
uc010snn.2. human. [P36896-4]

Organism-specific databases

CTDi91.
GeneCardsiGC12P052375.
HGNCiHGNC:172. ACVR1B.
HPAiCAB026126.
HPA063761.
MIMi601300. gene.
neXtProtiNX_P36896.
PharmGKBiPA24493.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118876.
HOGENOMiHOG000230587.
HOVERGENiHBG054502.
InParanoidiP36896.
KOiK13567.
OMAiNTHCCYE.
OrthoDBiEOG7Q8CN3.
PhylomeDBiP36896.
TreeFamiTF314724.

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_111057. Signaling by NODAL.
REACT_111059. Regulation of signaling by NODAL.
REACT_150238. Signaling by Activin.
SignaLinkiP36896.

Miscellaneous databases

GeneWikiiACVR1B.
GenomeRNAii91.
NextBioi339.
PROiP36896.
SOURCEiSearch...

Gene expression databases

BgeeiP36896.
CleanExiHS_ACVR1B.
ExpressionAtlasiP36896. baseline and differential.
GenevisibleiP36896. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR000472. TFB_recept_I/II_C.
IPR003605. TGF_beta_rcpt_GS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PfamiPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
SMARTiSM00467. GS. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity."
    ten Dijke P., Ichijo H., Franzen P., Schulz P., Saras J., Toyoshima H., Heldin C.-H., Miyazono K.
    Oncogene 8:2879-2887(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Type I receptors specify growth-inhibitory and transcriptional responses to transforming growth factor beta and activin."
    Carcamo J., Weis F.M., Ventura F., Wieser R., Wrana J.L., Attisano L., Massague J.
    Mol. Cell. Biol. 14:3810-3821(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION IN A ACTIVIN RECEPTOR COMPLEX, ACTIVIN-BINDING, FUNCTION.
    Tissue: Kidney.
  3. "Genomic structure and cloned cDNAs predict that four variants in the kinase domain of serine/threonine kinase receptors arise by alternative splicing and poly(A) addition."
    Xu J., Matsuzaki K., McKeehan K., Wang F., Kan M., McKeehan W.L.
    Proc. Natl. Acad. Sci. U.S.A. 91:7957-7961(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3), ALTERNATIVE SPLICING.
    Tissue: Liver.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain and Eye.
  8. "Activation of signalling by the activin receptor complex."
    Attisano L., Wrana J.L., Montalvo E., Massague J.
    Mol. Cell. Biol. 16:1066-1073(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACVR2B, PHOSPHORYLATION BY ACVR2B, DOMAIN GS, MUTAGENESIS OF THR-206.
  9. "Activin and inhibin have antagonistic effects on ligand-dependent heteromerization of the type I and type II activin receptors and human erythroid differentiation."
    Lebrun J.J., Vale W.W.
    Mol. Cell. Biol. 17:1682-1691(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, FUNCTION.
  10. "Roles of pathway-specific and inhibitory Smads in activin receptor signaling."
    Lebrun J.J., Takabe K., Chen Y., Vale W.
    Mol. Endocrinol. 13:15-23(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMAD2; SMAD3 AND SMAD7, FUNCTION.
  11. "Modulation of activin signal transduction by inhibin B and inhibin-binding protein (INhBP)."
    Chapman S.C., Woodruff T.K.
    Mol. Endocrinol. 15:668-679(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGSF1, ENZYME REGULATION.
  12. "Phosphorylation regulation of the interaction between Smad7 and activin type I receptor."
    Liu X., Nagarajan R.P., Vale W., Chen Y.
    FEBS Lett. 519:93-98(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH SMAD7.
  13. "Overexpression of wild-type activin receptor alk4-1 restores activin antiproliferative effects in human pituitary tumor cells."
    Danila D.C., Zhang X., Zhou Y., Haidar J.N., Klibanski A.
    J. Clin. Endocrinol. Metab. 87:4741-4746(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION.
  14. "Cripto-1 activates nodal- and ALK4-dependent and -independent signaling pathways in mammary epithelial Cells."
    Bianco C., Adkins H.B., Wechselberger C., Seno M., Normanno N., De Luca A., Sun Y., Khan N., Kenney N., Ebert A., Williams K.P., Sanicola M., Salomon D.S.
    Mol. Cell. Biol. 22:2586-2597(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TDGF1, ENZYME REGULATION.
  15. "Identification of the phosphotyrosine proteome from thrombin activated platelets."
    Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G., Fitzgerald D.J.
    Proteomics 2:642-648(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-380.
  16. "Activin signaling through type IB activin receptor stimulates aromatase activity in the ovarian granulosa cell-like human granulosa (KGN) cells."
    Mukasa C., Nomura M., Tanaka T., Tanaka K., Nishi Y., Okabe T., Goto K., Yanase T., Nawata H.
    Endocrinology 144:1603-1611(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Identification of a functional binding site for activin on the type I receptor ALK4."
    Harrison C.A., Gray P.C., Koerber S.C., Fischer W., Vale W.
    J. Biol. Chem. 278:21129-21135(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-40; ILE-70; VAL-73; LEU-75 AND PRO-77, ACTIVIN-BINDING.
  18. "FKBP12 functions as an adaptor of the Smad7-Smurf1 complex on activin type I receptor."
    Yamaguchi T., Kurisaki A., Yamakawa N., Minakuchi K., Sugino H.
    J. Mol. Endocrinol. 36:569-579(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FKBP1A AND SMAD7, UBIQUITINATION.
  19. "Ttrap is an essential modulator of Smad3-dependent Nodal signaling during zebrafish gastrulation and left-right axis determination."
    Esguerra C.V., Nelles L., Vermeire L., Ibrahimi A., Crawford A.D., Derua R., Janssens E., Waelkens E., Carmeliet P., Collen D., Huylebroeck D.
    Development 134:4381-4393(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOPHOSPHORYLATION.
  20. "Activin A induces neuronal differentiation and survival via ALK4 in a SMAD-independent manner in a subpopulation of human neuroblastomas."
    Suzuki K., Kobayashi T., Funatsu O., Morita A., Ikekita M.
    Biochem. Biophys. Res. Commun. 394:639-645(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Development and validation of a method for profiling post-translational modification activities using protein microarrays."
    Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
    PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  22. Cited for: INVOLVEMENT IN SYSTEMIC SCLEROSIS.
  23. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-146, VARIANT [LARGE SCALE ANALYSIS] HIS-478 (ISOFORM 3).

Entry informationi

Entry nameiACV1B_HUMAN
AccessioniPrimary (citable) accession number: P36896
Secondary accession number(s): B7Z5L8
, B7Z5W5, Q15479, Q15480, Q15481, Q15482
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 24, 2015
This is version 176 of the entry and version 1 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.