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P36896

- ACV1B_HUMAN

UniProt

P36896 - ACV1B_HUMAN

Protein

Activin receptor type-1B

Gene

ACVR1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    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

    Magnesium or manganese.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

    1. activin receptor activity, type I Source: UniProtKB
    2. ATP binding Source: HGNC
    3. inhibin binding Source: BHF-UCL
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: UniProtKB
    6. protein serine/threonine kinase activity Source: UniProtKB
    7. receptor signaling protein serine/threonine kinase activity Source: Ensembl
    8. SMAD binding Source: HGNC
    9. transforming growth factor beta-activated receptor activity Source: InterPro
    10. transmembrane receptor protein serine/threonine kinase activity Source: HGNC
    11. ubiquitin protein ligase binding Source: BHF-UCL

    GO - Biological processi

    1. activin receptor signaling pathway Source: UniProtKB
    2. central nervous system development Source: Ensembl
    3. development of primary female sexual characteristics Source: Ensembl
    4. extrinsic apoptotic signaling pathway Source: BHF-UCL
    5. G1/S transition of mitotic cell cycle Source: HGNC
    6. hair follicle development Source: Ensembl
    7. in utero embryonic development Source: Ensembl
    8. negative regulation of cell growth Source: HGNC
    9. nodal signaling pathway Source: UniProtKB
    10. peptidyl-threonine phosphorylation Source: UniProtKB
    11. positive regulation of activin receptor signaling pathway Source: BHF-UCL
    12. positive regulation of erythrocyte differentiation Source: HGNC
    13. positive regulation of pathway-restricted SMAD protein phosphorylation Source: Ensembl
    14. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    15. positive regulation of trophoblast cell migration Source: BHF-UCL
    16. protein autophosphorylation Source: UniProtKB
    17. protein phosphorylation Source: HGNC
    18. regulation of transcription, DNA-templated Source: HGNC
    19. signal transduction Source: HGNC
    20. transmembrane receptor protein serine/threonine kinase signaling pathway Source: ProtInc

    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: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:172. ACVR1B.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: HGNC
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of plasma membrane Source: HGNC
    4. plasma membrane Source: Reactome

    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.

    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

    ArrayExpressiP36896.
    BgeeiP36896.
    CleanExiHS_ACVR1B.
    GenevestigatoriP36896.

    Organism-specific databases

    HPAiCAB026126.

    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. 28 interactions.
    DIPiDIP-427N.
    IntActiP36896. 8 interactions.
    STRINGi9606.ENSP00000257963.

    Structurei

    3D structure databases

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

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei127 – 14923HelicalSequence AnalysisAdd
    BLAST

    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.
    HOGENOMiHOG000230587.
    HOVERGENiHBG054502.
    InParanoidiP36896.
    KOiK13567.
    OMAiQCACTSC.
    OrthoDBiEOG7Q8CN3.
    PhylomeDBiP36896.
    TreeFamiTF314724.

    Family and domain databases

    InterProiIPR000472. Activin_rcpt.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    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. Align

    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

    MAESAGASSF FPLVVLLLAG SGGSGPRGVQ ALLCACTSCL QANYTCETDG    50
    ACMVSIFNLD GMEHHVRTCI PKVELVPAGK PFYCLSSEDL RNTHCCYTDY 100
    CNRIDLRVPS GHLKEPEHPS MWGPVELVGI IAGPVFLLFL IIIIVFLVIN 150
    YHQRVYHNRQ RLDMEDPSCE MCLSKDKTLQ DLVYDLSTSG SGSGLPLFVQ 200
    RTVARTIVLQ EIIGKGRFGE VWRGRWRGGD VAVKIFSSRE ERSWFREAEI 250
    YQTVMLRHEN ILGFIAADNK DNGTWTQLWL VSDYHEHGSL FDYLNRYTVT 300
    IEGMIKLALS AASGLAHLHM EIVGTQGKPG IAHRDLKSKN ILVKKNGMCA 350
    IADLGLAVRH DAVTDTIDIA PNQRVGTKRY MAPEVLDETI NMKHFDSFKC 400
    ADIYALGLVY WEIARRCNSG GVHEEYQLPY YDLVPSDPSI EEMRKVVCDQ 450
    KLRPNIPNWW QSYEALRVMG KMMRECWYAN GAARLTALRI KKTLSQLSVQ 500
    EDVKI 505
    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi547775.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS44893.2. [P36896-5 ]
    CCDS44894.2. [P36896-4 ]
    CCDS8816.1. [P36896-1 ]
    PIRi I38859.
    I80182.
    I80183.
    RefSeqi NP_004293.1. NM_004302.4. [P36896-1 ]
    NP_064732.3. NM_020327.3. [P36896-5 ]
    NP_064733.3. NM_020328.3. [P36896-4 ]
    UniGenei Hs.438918.

    3D structure databases

    ProteinModelPortali P36896.
    SMRi P36896. Positions 31-104, 149-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106606. 28 interactions.
    DIPi DIP-427N.
    IntActi P36896. 8 interactions.
    STRINGi 9606.ENSP00000257963.

    Chemistry

    BindingDBi P36896.
    ChEMBLi CHEMBL5310.
    DrugBanki DB00171. Adenosine triphosphate.
    GuidetoPHARMACOLOGYi 1787.

    PTM databases

    PhosphoSitei P36896.

    Polymorphism databases

    DMDMi 547775.

    Proteomic databases

    MaxQBi P36896.
    PaxDbi P36896.
    PRIDEi P36896.

    Protocols and materials databases

    DNASUi 91.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257963 ; ENSP00000257963 ; ENSG00000135503 . [P36896-1 ]
    ENST00000415850 ; ENSP00000397550 ; ENSG00000135503 . [P36896-3 ]
    ENST00000426655 ; ENSP00000390477 ; ENSG00000135503 . [P36896-2 ]
    ENST00000541224 ; ENSP00000442656 ; ENSG00000135503 . [P36896-4 ]
    ENST00000542485 ; ENSP00000442885 ; ENSG00000135503 . [P36896-5 ]
    GeneIDi 91.
    KEGGi hsa:91.
    UCSCi uc001rzl.3. human. [P36896-3 ]
    uc001rzm.3. human. [P36896-2 ]
    uc001rzn.3. human. [P36896-1 ]
    uc010snn.2. human. [P36896-4 ]

    Organism-specific databases

    CTDi 91.
    GeneCardsi GC12P052375.
    HGNCi HGNC:172. ACVR1B.
    HPAi CAB026126.
    MIMi 601300. gene.
    neXtProti NX_P36896.
    PharmGKBi PA24493.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000230587.
    HOVERGENi HBG054502.
    InParanoidi P36896.
    KOi K13567.
    OMAi QCACTSC.
    OrthoDBi EOG7Q8CN3.
    PhylomeDBi P36896.
    TreeFami TF314724.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_111057. Signaling by NODAL.
    REACT_111059. Regulation of signaling by NODAL.
    REACT_150238. Signaling by Activin.
    SignaLinki P36896.

    Miscellaneous databases

    GeneWikii ACVR1B.
    GenomeRNAii 91.
    NextBioi 339.
    PROi P36896.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P36896.
    Bgeei P36896.
    CleanExi HS_ACVR1B.
    Genevestigatori P36896.

    Family and domain databases

    InterProi IPR000472. Activin_rcpt.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    IPR003605. TGF_beta_rcpt_GS.
    IPR000333. TGFB_receptor.
    [Graphical view ]
    PANTHERi PTHR23255. PTHR23255. 1 hit.
    Pfami PF01064. Activin_recp. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF08515. TGF_beta_GS. 1 hit.
    [Graphical view ]
    SMARTi SM00467. GS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51256. GS. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 168 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