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UniProtKB/Swiss-Prot entry Q04771


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACVR1_HUMAN
Primary accession number Q04771
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on February 1, 1994 (Sequence version 1)
Annotations were last modified on    June 10, 2008 (Entry version 90)
Name and origin of the protein
Protein name Activin receptor type-1 [Precursor]
Synonyms EC 2.7.11.30
Activin receptor type I
ACTR-I
Serine/threonine-protein kinase receptor R1
SKR1
Activin receptor-like kinase 2
ALK-2
TGF-B superfamily receptor type I
TSR-I
Gene name
Name: ACVR1
Synonyms: ACVRLK2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8389764 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuzaki K., McKeehan W.L.;
"A widely expressed transmembrane serine/threonine kinase that does not bind activin, inhibin, transforming growth factor beta, or bone morphogenic factor.";
J. Biol. Chem. 268:12719-12723(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8397373 [NCBI, ExPASy, EBI, Israel, Japan]
ten Dijke P., Ichijo H., Franzen P., Schulz P., Saras J., Toyoshima H., Heldin C.-H., Miyazono K.;
"Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity.";
Oncogene 8:2879-2887(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[5]
VARIANT FOP HIS-206.
DOI=10.1038/ng1783; PubMed=16642017 [NCBI, ExPASy, EBI, Israel, Japan]
Shore E.M., Xu M., Feldman G.J., Fenstermacher D.A., Brown M.A., Kaplan F.S.;
"A recurrent mutation in the BMP type I receptor ACVR1 causes inherited and sporadic fibrodysplasia ossificans progressiva.";
Nat. Genet. 38:525-527(2006).
[6]
VARIANTS [LARGE SCALE ANALYSIS] GLY-15; PHE-41; GLN-47 AND SER-115.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L02911; AAA36614.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z22534; CAA80256.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC033867; AAH33867.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A45992; A45992.
RefSeq NP_001096.1; -.
NP_001104537.1; -.
UniGene Hs.470316
3D structure databases
HSSP P36897; 1IAS. [HSSP ENTRY / PDB]
ModBase Q04771.
Protein-protein interaction databases
DIP DIP:212N; -.
IntAct Q04771; -.
Organism-specific databases
H-InvDB HIX0002524; -.
HGNC HGNC:171; ACVR1.
GeneLynx ACVR1; Homo sapiens.
GenAtlas ACVR1.
MIM 102576; gene. [NCBI / EBI]
135100; phenotype. [NCBI / EBI]
Orphanet 337; Fibrodysplasia ossificans progressiva.
PharmGKB PA24492; -.
GeneCards Q04771.
Gene expression databases
ArrayExpress Q04771; -.
CleanEx HS_ACVR1; -.
GermOnline ENSG00000115170; Homo sapiens.
Ontologies
GO
GO:0048179; Cellular component: activin receptor complex (inferred from direct assay from UniProtKB).
GO:0048185; Molecular function: activin binding (inferred from direct assay from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred from direct assay from HGNC).
GO:0048184; Molecular function: follistatin binding (non-traceable author statement from UniProtKB).
GO:0046332; Molecular function: SMAD binding (inferred from direct assay from HGNC).
GO:0050431; Molecular function: transforming growth factor beta binding (inferred from direct assay from UniProtKB).
GO:0000082; Biological process: G1/S transition of mitotic cell cycle (inferred from mutant phenotype from HGNC).
GO:0032926; Biological process: negative regulation of activin receptor signaling pathway (inferred from mutant phenotype from HGNC).
GO:0043066; Biological process: negative regulation of apoptosis (inferred from mutant phenotype from HGNC).
GO:0045941; Biological process: positive regulation of transcription (inferred from direct assay from UniProtKB).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from direct assay from HGNC).
GO:0030278; Biological process: regulation of ossification (inferred from mutant phenotype from UniProtKB).
GO:0007179; Biological process: transforming growth factor beta receptor signaling pathway (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000333; Activin_II_recpt.
IPR000472; Activin_rcpt.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR008271; Ser_thr_pkin_AS.
IPR003605; TGF_beta_rcpt_GS.
Graphical view of domain structure.
Pfam PF01064; Activin_recp; 1.
PF08515; TGF_beta_GS; 1.
Pfam graphical view of domain structure.
PRINTS PR00653; ACTIVIN2R.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00467; GS; 1.
SMART graphical view of domain structure.
PROSITE PS51256; GS; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q04771.
Genome annotation databases
Ensembl ENSG00000115170; Homo sapiens. [Contig view]
GeneID 90; -.
KEGG hsa:90; -.
Phylogenomic databases
HOGENOM Q04771; -.
HOVERGEN Q04771; -.
Other
DrugBank DB00171; Adenosine triphosphate.
SOURCE ACVR1; Homo sapiens.
ProtoNet Q04771.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Disease mutation; Glycoprotein; Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor; Serine/threonine-protein kinase; Signal; Transferase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20     By similarity. 
CHAIN   21   509  489     Activin receptor type-1. PRO_0000024394
TOPO_DOM   21   123  103     Extracellular (Potential). 
TRANSMEM   124   146  23     Potential. 
TOPO_DOM   147   509  363     Cytoplasmic (Potential). 
DOMAIN   178   207  30     GS. 
DOMAIN   208   502  295     Protein kinase. 
NP_BIND   214   222  9     ATP (By similarity). 
ACT_SITE   336   336        Proton acceptor (By similarity). 
BINDING   235   235        ATP (By similarity). 
MOD_RES   501   501        Phosphoserine. 
CARBOHYD   102   102        N-linked (GlcNAc...) (Potential). 
VARIANT   15    15  1     A -> G. VAR_041392 
VARIANT   41    41  1     S -> F. VAR_041393 
VARIANT   47    47  1     H -> Q. VAR_041394 
VARIANT   115   115  1     P -> S (in a melanoma sample; somatic mutation). VAR_041395 
VARIANT   206   206  1     R -> H (in FOP). VAR_028444 
Sequence information
Length: 509 AA [This is the length of the unprocessed precursor] Molecular weight: 57153 Da [This is the MW of the unprocessed precursor] CRC64: E2B0F051D19DD052 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVDGVMILPV LIMIALPSPS MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN 

        70         80         90        100        110        120 
DGFHVYQKGC FQVYEQGKMT CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF 

       130        140        150        160        170        180 
HLEVGLIILS VVFAVCLLAC LLGVALRKFK RRNQERLNPR DVEYGTIEGL ITTNVGDSTL 

       190        200        210        220        230        240 
ADLLDHSCTS GSGSGLPFLV QRTVARQITL LECVGKGRYG EVWRGSWQGE NVAVKIFSSR 

       250        260        270        280        290        300 
DEKSWFRETE LYNTVMLRHE NILGFIASDM TSRHSSTQLW LITHYHEMGS LYDYLQLTTL 

       310        320        330        340        350        360 
DTVSCLRIVL SIASGLAHLH IEIFGTQGKP AIAHRDLKSK NILVKKNGQC CIADLGLAVM 

       370        380        390        400        410        420 
HSQSTNQLDV GNNPRVGTKR YMAPEVLDET IQVDCFDSYK RVDIWAFGLV LWEVARRMVS 

       430        440        450        460        470        480 
NGIVEDYKPP FYDVVPNDPS FEDMRKVVCV DQQRPNIPNR WFSDPTLTSL AKLMKECWYQ 

       490        500 
NPSARLTALR IKKTLTKIDN SLDKLKTDC 

Q04771 in FASTA format

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