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Q04771

- ACVR1_HUMAN

UniProt

Q04771 - ACVR1_HUMAN

Protein

Activin receptor type-1

Gene

ACVR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin. May be involved for left-right pattern formation during embryogenesis By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Magnesium or manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei235 – 2351ATPPROSITE-ProRule annotation
    Active sitei336 – 3361Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi214 – 2229ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. activin binding Source: UniProtKB
    2. activin receptor activity, type I Source: Ensembl
    3. ATP binding Source: HGNC
    4. metal ion binding Source: UniProtKB-KW
    5. peptide hormone binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. protein homodimerization activity Source: BHF-UCL
    8. protein kinase activity Source: BHF-UCL
    9. protein serine/threonine kinase activity Source: HGNC
    10. receptor signaling protein serine/threonine kinase activity Source: Ensembl
    11. SMAD binding Source: HGNC
    12. transforming growth factor beta binding Source: UniProtKB
    13. transforming growth factor beta receptor activity, type I Source: Ensembl

    GO - Biological processi

    1. activin receptor signaling pathway Source: BHF-UCL
    2. acute inflammatory response Source: Ensembl
    3. atrial septum primum morphogenesis Source: BHF-UCL
    4. BMP signaling pathway Source: BHF-UCL
    5. cardiac muscle cell fate commitment Source: BHF-UCL
    6. cellular response to glucocorticoid stimulus Source: Ensembl
    7. determination of left/right symmetry Source: Ensembl
    8. embryonic heart tube morphogenesis Source: BHF-UCL
    9. endocardial cushion cell fate commitment Source: BHF-UCL
    10. G1/S transition of mitotic cell cycle Source: HGNC
    11. gastrulation with mouth forming second Source: Ensembl
    12. germ cell development Source: Ensembl
    13. in utero embryonic development Source: Ensembl
    14. mesoderm formation Source: Ensembl
    15. mitral valve morphogenesis Source: BHF-UCL
    16. negative regulation of activin receptor signaling pathway Source: HGNC
    17. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
    18. negative regulation of signal transduction Source: HGNC
    19. neural crest cell migration Source: Ensembl
    20. pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
    21. patterning of blood vessels Source: Ensembl
    22. peptidyl-threonine phosphorylation Source: BHF-UCL
    23. pharyngeal system development Source: Ensembl
    24. positive regulation of bone mineralization Source: BHF-UCL
    25. positive regulation of determination of dorsal identity Source: BHF-UCL
    26. positive regulation of osteoblast differentiation Source: BHF-UCL
    27. positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
    28. positive regulation of transcription, DNA-templated Source: UniProtKB
    29. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    30. protein phosphorylation Source: BHF-UCL
    31. regulation of ossification Source: UniProtKB
    32. regulation of skeletal muscle tissue development Source: Ensembl
    33. smooth muscle cell differentiation Source: Ensembl
    34. transforming growth factor beta receptor signaling pathway Source: UniProtKB
    35. urogenital system development Source: Ensembl

    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.
    SignaLinkiQ04771.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Activin receptor type-1 (EC:2.7.11.30)
    Alternative name(s):
    Activin receptor type I
    Short name:
    ACTR-I
    Activin receptor-like kinase 2
    Short name:
    ALK-2
    Serine/threonine-protein kinase receptor R1
    Short name:
    SKR1
    TGF-B superfamily receptor type I
    Short name:
    TSR-I
    Gene namesi
    Name:ACVR1
    Synonyms:ACVRLK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:171. ACVR1.

    Subcellular locationi

    GO - Cellular componenti

    1. activin receptor complex Source: UniProtKB
    2. apical part of cell Source: Ensembl
    3. integral component of plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Fibrodysplasia ossificans progressiva (FOP) [MIM:135100]: A rare autosomal dominant connective tissue disorder resulting in skeletal malformations and progressive extraskeletal ossification. Heterotopic ossification begins in childhood and can be induced by trauma or may occur without warning. Bone formation is episodic and progressive, leading to a debilitating ankylosis of all major joints of the axial and appendicular skeleton, rendering movement impossible.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti197 – 1982PF → L in FOP; variant phenotype.
    VAR_058418
    Natural varianti202 – 2021R → I in FOP; with some atypical features. 1 Publication
    VAR_058419
    Natural varianti206 – 2061R → H in FOP. 2 Publications
    VAR_028444
    Natural varianti207 – 2071Q → E in FOP; with some atypical features. 1 Publication
    VAR_058420
    Natural varianti328 – 3281G → E in FOP; variant phenotype. 2 Publications
    VAR_058421
    Natural varianti328 – 3281G → R in FOP; variant phenotype. 1 Publication
    VAR_058422
    Natural varianti328 – 3281G → W in FOP; variant phenotype. 1 Publication
    VAR_058423
    Natural varianti356 – 3561G → D in FOP; variant phenotype. 1 Publication
    VAR_058424
    Natural varianti375 – 3751R → P in FOP; variant phenotype. 1 Publication
    VAR_058425

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi135100. phenotype.
    Orphaneti337. Fibrodysplasia ossificans progressiva.
    PharmGKBiPA24492.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020By similarityAdd
    BLAST
    Chaini21 – 509489Activin receptor type-1PRO_0000024394Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
    Modified residuei501 – 5011Phosphoserine1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ04771.
    PaxDbiQ04771.
    PRIDEiQ04771.

    PTM databases

    PhosphoSiteiQ04771.

    Expressioni

    Tissue specificityi

    Expressed in normal parenchymal cells, endothelial cells, fibroblasts and tumor-derived epithelial cells.

    Gene expression databases

    ArrayExpressiQ04771.
    BgeeiQ04771.
    CleanExiHS_ACVR1.
    GenevestigatoriQ04771.

    Organism-specific databases

    HPAiHPA007505.
    HPA046514.

    Interactioni

    Subunit structurei

    Interacts with FKBP1A. Interacts with FCHO1.2 Publications

    Protein-protein interaction databases

    BioGridi106605. 60 interactions.
    DIPiDIP-212N.
    IntActiQ04771. 1 interaction.
    MINTiMINT-1340145.
    STRINGi9606.ENSP00000263640.

    Structurei

    Secondary structure

    1
    509
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi180 – 1845
    Beta strandi192 – 1965
    Helixi205 – 2073
    Beta strandi209 – 2168
    Beta strandi218 – 22710
    Beta strandi230 – 2378
    Helixi239 – 2413
    Helixi242 – 25413
    Beta strandi265 – 2739
    Beta strandi276 – 2838
    Helixi291 – 2955
    Helixi302 – 32019
    Beta strandi325 – 3273
    Beta strandi331 – 3333
    Helixi339 – 3413
    Beta strandi342 – 3443
    Beta strandi350 – 3523
    Beta strandi359 – 3624
    Turni363 – 3664
    Beta strandi367 – 3693
    Helixi379 – 3813
    Helixi384 – 3874
    Helixi396 – 41520
    Turni430 – 4345
    Helixi441 – 4488
    Helixi459 – 4635
    Helixi465 – 47713
    Helixi482 – 4843
    Helixi488 – 49811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3H9RX-ray2.35A172-499[»]
    3MTFX-ray2.15A/B201-499[»]
    3OOMX-ray2.00A201-499[»]
    3Q4UX-ray1.82A/B/C/D201-499[»]
    4BGGX-ray2.56A/B/C/D201-499[»]
    4C02X-ray2.17A172-499[»]
    4DYMX-ray2.42A201-499[»]
    ProteinModelPortaliQ04771.
    SMRiQ04771. Positions 143-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04771.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 123103ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini147 – 509363CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei124 – 14623HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini178 – 20730GSPROSITE-ProRule annotationAdd
    BLAST
    Domaini208 – 502295Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    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.
    InParanoidiQ04771.
    KOiK04675.
    OMAiVCEGMSC.
    OrthoDBiEOG7Q8CN3.
    PhylomeDBiQ04771.
    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]
    PRINTSiPR00653. ACTIVIN2R.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    Q04771-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDGVMILPV LIMIALPSPS MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG    50
    QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT CKTPPSPGQA VECCQGDWCN 100
    RNITAQLPTK GKSFPGTQNF HLEVGLIILS VVFAVCLLAC LLGVALRKFK 150
    RRNQERLNPR DVEYGTIEGL ITTNVGDSTL ADLLDHSCTS GSGSGLPFLV 200
    QRTVARQITL LECVGKGRYG EVWRGSWQGE NVAVKIFSSR DEKSWFRETE 250
    LYNTVMLRHE NILGFIASDM TSRHSSTQLW LITHYHEMGS LYDYLQLTTL 300
    DTVSCLRIVL SIASGLAHLH IEIFGTQGKP AIAHRDLKSK NILVKKNGQC 350
    CIADLGLAVM HSQSTNQLDV GNNPRVGTKR YMAPEVLDET IQVDCFDSYK 400
    RVDIWAFGLV LWEVARRMVS NGIVEDYKPP FYDVVPNDPS FEDMRKVVCV 450
    DQQRPNIPNR WFSDPTLTSL AKLMKECWYQ NPSARLTALR IKKTLTKIDN 500
    SLDKLKTDC 509
    Length:509
    Mass (Da):57,153
    Last modified:February 1, 1994 - v1
    Checksum:iE2B0F051D19DD052
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151A → G.1 Publication
    Corresponds to variant rs13406336 [ dbSNP | Ensembl ].
    VAR_041392
    Natural varianti41 – 411S → F.1 Publication
    Corresponds to variant rs55957214 [ dbSNP | Ensembl ].
    VAR_041393
    Natural varianti47 – 471H → Q.1 Publication
    Corresponds to variant rs34056189 [ dbSNP | Ensembl ].
    VAR_041394
    Natural varianti115 – 1151P → S in a melanoma sample; somatic mutation. 1 Publication
    VAR_041395
    Natural varianti197 – 1982PF → L in FOP; variant phenotype.
    VAR_058418
    Natural varianti202 – 2021R → I in FOP; with some atypical features. 1 Publication
    VAR_058419
    Natural varianti206 – 2061R → H in FOP. 2 Publications
    VAR_028444
    Natural varianti207 – 2071Q → E in FOP; with some atypical features. 1 Publication
    VAR_058420
    Natural varianti328 – 3281G → E in FOP; variant phenotype. 2 Publications
    VAR_058421
    Natural varianti328 – 3281G → R in FOP; variant phenotype. 1 Publication
    VAR_058422
    Natural varianti328 – 3281G → W in FOP; variant phenotype. 1 Publication
    VAR_058423
    Natural varianti356 – 3561G → D in FOP; variant phenotype. 1 Publication
    VAR_058424
    Natural varianti375 – 3751R → P in FOP; variant phenotype. 1 Publication
    VAR_058425

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02911 mRNA. Translation: AAA36614.1.
    Z22534 mRNA. Translation: CAA80256.1.
    BC033867 mRNA. Translation: AAH33867.1.
    CCDSiCCDS2206.1.
    PIRiA45992.
    RefSeqiNP_001096.1. NM_001105.4.
    NP_001104537.1. NM_001111067.2.
    XP_005246996.1. XM_005246939.1.
    XP_005246997.1. XM_005246940.1.
    XP_006712888.1. XM_006712825.1.
    UniGeneiHs.470316.

    Genome annotation databases

    EnsembliENST00000263640; ENSP00000263640; ENSG00000115170.
    ENST00000409283; ENSP00000387273; ENSG00000115170.
    ENST00000410057; ENSP00000387127; ENSG00000115170.
    ENST00000434821; ENSP00000405004; ENSG00000115170.
    GeneIDi90.
    KEGGihsa:90.
    UCSCiuc002tzm.3. human.

    Polymorphism databases

    DMDMi462447.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02911 mRNA. Translation: AAA36614.1 .
    Z22534 mRNA. Translation: CAA80256.1 .
    BC033867 mRNA. Translation: AAH33867.1 .
    CCDSi CCDS2206.1.
    PIRi A45992.
    RefSeqi NP_001096.1. NM_001105.4.
    NP_001104537.1. NM_001111067.2.
    XP_005246996.1. XM_005246939.1.
    XP_005246997.1. XM_005246940.1.
    XP_006712888.1. XM_006712825.1.
    UniGenei Hs.470316.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3H9R X-ray 2.35 A 172-499 [» ]
    3MTF X-ray 2.15 A/B 201-499 [» ]
    3OOM X-ray 2.00 A 201-499 [» ]
    3Q4U X-ray 1.82 A/B/C/D 201-499 [» ]
    4BGG X-ray 2.56 A/B/C/D 201-499 [» ]
    4C02 X-ray 2.17 A 172-499 [» ]
    4DYM X-ray 2.42 A 201-499 [» ]
    ProteinModelPortali Q04771.
    SMRi Q04771. Positions 143-499.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106605. 60 interactions.
    DIPi DIP-212N.
    IntActi Q04771. 1 interaction.
    MINTi MINT-1340145.
    STRINGi 9606.ENSP00000263640.

    Chemistry

    BindingDBi Q04771.
    ChEMBLi CHEMBL5903.
    DrugBanki DB00171. Adenosine triphosphate.
    GuidetoPHARMACOLOGYi 1785.

    PTM databases

    PhosphoSitei Q04771.

    Polymorphism databases

    DMDMi 462447.

    Proteomic databases

    MaxQBi Q04771.
    PaxDbi Q04771.
    PRIDEi Q04771.

    Protocols and materials databases

    DNASUi 90.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263640 ; ENSP00000263640 ; ENSG00000115170 .
    ENST00000409283 ; ENSP00000387273 ; ENSG00000115170 .
    ENST00000410057 ; ENSP00000387127 ; ENSG00000115170 .
    ENST00000434821 ; ENSP00000405004 ; ENSG00000115170 .
    GeneIDi 90.
    KEGGi hsa:90.
    UCSCi uc002tzm.3. human.

    Organism-specific databases

    CTDi 90.
    GeneCardsi GC02M158594.
    HGNCi HGNC:171. ACVR1.
    HPAi HPA007505.
    HPA046514.
    MIMi 102576. gene.
    135100. phenotype.
    neXtProti NX_Q04771.
    Orphaneti 337. Fibrodysplasia ossificans progressiva.
    PharmGKBi PA24492.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000230587.
    HOVERGENi HBG054502.
    InParanoidi Q04771.
    KOi K04675.
    OMAi VCEGMSC.
    OrthoDBi EOG7Q8CN3.
    PhylomeDBi Q04771.
    TreeFami TF314724.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    SignaLinki Q04771.

    Miscellaneous databases

    EvolutionaryTracei Q04771.
    GeneWikii ACVR1.
    GenomeRNAii 90.
    NextBioi 335.
    PROi Q04771.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q04771.
    Bgeei Q04771.
    CleanExi HS_ACVR1.
    Genevestigatori Q04771.

    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 ]
    PRINTSi PR00653. ACTIVIN2R.
    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. "A widely expressed transmembrane serine/threonine kinase that does not bind activin, inhibin, transforming growth factor beta, or bone morphogenic factor."
      Matsuzaki K., McKeehan W.L.
      J. Biol. Chem. 268:12719-12723(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
      Tissue: Placenta.
    3. "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].
      Tissue: Lung.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning."
      Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M.
      Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FCHO1.
    6. "Crystal structure of the kinase domain of type I activin receptor (ACVR1) in complex with FKBP12 and dorsomorphin."
      Structural genomics consortium (SGC)
      Submitted (JUN-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 172-499 IN COMPLEX WITH FKBP1A.
    7. "A recurrent mutation in the BMP type I receptor ACVR1 causes inherited and sporadic fibrodysplasia ossificans progressiva."
      Shore E.M., Xu M., Feldman G.J., Fenstermacher D.A., Brown M.A., Kaplan F.S.
      Nat. Genet. 38:525-527(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FOP HIS-206.
    8. "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: VARIANTS [LARGE SCALE ANALYSIS] GLY-15; PHE-41; GLN-47 AND SER-115.
    9. "Classic and atypical fibrodysplasia ossificans progressiva (FOP) phenotypes are caused by mutations in the bone morphogenetic protein (BMP) type I receptor ACVR1."
      Kaplan F.S., Xu M., Seemann P., Connor J.M., Glaser D.L., Carroll L., Delai P., Fastnacht-Urban E., Forman S.J., Gillessen-Kaesbach G., Hoover-Fong J., Koester B., Pauli R.M., Reardon W., Zaidi S.A., Zasloff M., Morhart R., Mundlos S., Groppe J., Shore E.M.
      Hum. Mutat. 30:379-390(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FOP 197-PRO-PHE-198 DELINS LEU; HIS-206; GLU-207; ARG-328; TRP-328; GLU-328; ASP-356 AND PRO-375.
    10. "Novel mutations in ACVR1 result in atypical features in two fibrodysplasia ossificans progressiva patients."
      Petrie K.A., Lee W.H., Bullock A.N., Pointon J.J., Smith R., Russell R.G., Brown M.A., Wordsworth B.P., Triffitt J.T.
      PLoS ONE 4:E5005-E5005(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FOP ILE-202 AND GLU-328.

    Entry informationi

    Entry nameiACVR1_HUMAN
    AccessioniPrimary (citable) accession number: Q04771
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 155 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3