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Activin receptor type-1 (EC 2.7.11.30) (Activin receptor type I) (ACTR-I) (Activin receptor-like kinase 2) (ALK-2) (Serine/threonine-protein kinase receptor R1) (SKR1) (TGF-B superfamily receptor type I) (TSR-I)

 ACVR1_HUMAN             Reviewed;         509 AA.
Q04771;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
17-JUN-2020, entry version 204.
RecName: Full=Activin receptor type-1;
EC=2.7.11.30;
AltName: Full=Activin receptor type I;
Short=ACTR-I;
AltName: Full=Activin receptor-like kinase 2;
Short=ALK-2;
AltName: Full=Serine/threonine-protein kinase receptor R1;
Short=SKR1;
AltName: Full=TGF-B superfamily receptor type I;
Short=TSR-I;
Flags: Precursor;
Name=ACVR1; Synonyms=ACVRLK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8389764;
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;
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;
PubMed=15489334; DOI=10.1101/gr.2596504;
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]
INTERACTION WITH CLU.
PubMed=8555189; DOI=10.1021/bi951880a;
Reddy K.B., Karode M.C., Harmony A.K., Howe P.H.;
"Interaction of transforming growth factor beta receptors with
apolipoprotein J/clusterin.";
Biochemistry 35:309-314(1996).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[6]
INTERACTION WITH FCHO1.
PubMed=22484487; DOI=10.1038/ncb2473;
Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
Tsang M., Traub L.M.;
"Distinct and separable activities of the endocytic clathrin-coat
components Fcho1/2 and AP-2 in developmental patterning.";
Nat. Cell Biol. 14:488-501(2012).
[7]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 172-499 IN COMPLEX WITH FKBP1A.
Structural genomics consortium (SGC);
"Crystal structure of the kinase domain of type I activin receptor (ACVR1)
in complex with FKBP12 and dorsomorphin.";
Submitted (JUN-2009) to the PDB data bank.
[8]
VARIANT FOP HIS-206.
PubMed=16642017; DOI=10.1038/ng1783;
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).
[9]
VARIANTS [LARGE SCALE ANALYSIS] GLY-15; PHE-41; GLN-47 AND SER-115.
PubMed=17344846; DOI=10.1038/nature05610;
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).
[10]
VARIANTS FOP 197-PRO-PHE-198 DELINS LEU; HIS-206; GLU-207; ARG-328;
TRP-328; GLU-328; ASP-356 AND PRO-375.
PubMed=19085907; DOI=10.1002/humu.20868;
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.;
"Classic and atypical fibrodysplasia ossificans progressiva (FOP)
phenotypes are caused by mutations in the bone morphogenetic protein (BMP)
type I receptor ACVR1.";
Hum. Mutat. 30:379-390(2009).
[11]
VARIANTS FOP ILE-202 AND GLU-328.
PubMed=19330033; DOI=10.1371/journal.pone.0005005;
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.;
"Novel mutations in ACVR1 result in atypical features in two fibrodysplasia
ossificans progressiva patients.";
PLoS ONE 4:E5005-E5005(2009).
-!- FUNCTION: 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). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=[receptor-protein]-L-threonine + ATP = [receptor-protein]-O-
phospho-L-threonine + ADP + H(+); Xref=Rhea:RHEA:44880, Rhea:RHEA-
COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
ChEBI:CHEBI:456216; EC=2.7.11.30;
-!- CATALYTIC ACTIVITY:
Reaction=[receptor-protein]-L-serine + ATP = [receptor-protein]-O-
phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA-
COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
ChEBI:CHEBI:456216; EC=2.7.11.30;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts with FKBP1A (PubMed:22484487, Ref.7). Interacts with
FCHO1 (PubMed:22484487). Interacts with CLU (PubMed:8555189).
{ECO:0000269|PubMed:22484487, ECO:0000269|PubMed:8555189,
ECO:0000269|Ref.7}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
-!- TISSUE SPECIFICITY: Expressed in normal parenchymal cells, endothelial
cells, fibroblasts and tumor-derived epithelial cells.
-!- DISEASE: 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.
{ECO:0000269|PubMed:16642017, ECO:0000269|PubMed:19085907,
ECO:0000269|PubMed:19330033}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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EMBL; L02911; AAA36614.1; -; mRNA.
EMBL; Z22534; CAA80256.1; -; mRNA.
EMBL; BC033867; AAH33867.1; -; mRNA.
CCDS; CCDS2206.1; -.
PIR; A45992; A45992.
RefSeq; NP_001096.1; NM_001105.4.
RefSeq; NP_001104537.1; NM_001111067.2.
RefSeq; NP_001334592.1; NM_001347663.1.
RefSeq; NP_001334593.1; NM_001347664.1.
RefSeq; NP_001334594.1; NM_001347665.1.
RefSeq; NP_001334595.1; NM_001347666.1.
RefSeq; NP_001334596.1; NM_001347667.1.
RefSeq; XP_006712888.1; XM_006712825.3.
RefSeq; XP_011510410.1; XM_011512108.2.
PDB; 3H9R; X-ray; 2.35 A; A=172-499.
PDB; 3MTF; X-ray; 2.15 A; A/B=201-499.
PDB; 3OOM; X-ray; 2.00 A; A=201-499.
PDB; 3Q4U; X-ray; 1.82 A; A/B/C/D=201-499.
PDB; 4BGG; X-ray; 2.56 A; A/B/C/D=201-499.
PDB; 4C02; X-ray; 2.17 A; A=172-499.
PDB; 4DYM; X-ray; 2.42 A; A=201-499.
PDB; 5OXG; X-ray; 2.13 A; A/B/C/D=201-499.
PDB; 5OY6; X-ray; 2.56 A; A/B/C/D=201-499.
PDB; 6ACR; X-ray; 2.01 A; A/B=201-499.
PDB; 6EIX; X-ray; 2.30 A; A=172-509.
PDB; 6GI6; X-ray; 1.98 A; A=201-499.
PDB; 6GIN; X-ray; 2.20 A; A/B=201-499.
PDB; 6GIP; X-ray; 2.17 A; A=201-499.
PDB; 6I1S; X-ray; 1.52 A; A=172-499.
PDB; 6SRH; X-ray; 1.25 A; A/B=201-499.
PDB; 6SZM; X-ray; 1.42 A; A/B=201-499.
PDB; 6T6D; X-ray; 2.56 A; A/B/C/D=201-499.
PDB; 6T8N; X-ray; 1.77 A; A/B=201-499.
PDB; 6TN8; X-ray; 1.63 A; A=201-499.
PDBsum; 3H9R; -.
PDBsum; 3MTF; -.
PDBsum; 3OOM; -.
PDBsum; 3Q4U; -.
PDBsum; 4BGG; -.
PDBsum; 4C02; -.
PDBsum; 4DYM; -.
PDBsum; 5OXG; -.
PDBsum; 5OY6; -.
PDBsum; 6ACR; -.
PDBsum; 6EIX; -.
PDBsum; 6GI6; -.
PDBsum; 6GIN; -.
PDBsum; 6GIP; -.
PDBsum; 6I1S; -.
PDBsum; 6SRH; -.
PDBsum; 6SZM; -.
PDBsum; 6T6D; -.
PDBsum; 6T8N; -.
PDBsum; 6TN8; -.
SMR; Q04771; -.
BioGRID; 106605; 84.
DIP; DIP-212N; -.
IntAct; Q04771; 15.
MINT; Q04771; -.
STRING; 9606.ENSP00000263640; -.
BindingDB; Q04771; -.
ChEMBL; CHEMBL5903; -.
DrugBank; DB08597; 6-[4-(2-piperidin-1-ylethoxy)phenyl]-3-pyridin-4-ylpyrazolo[1,5-a]pyrimidine.
DrugBank; DB00171; ATP.
DrugBank; DB12010; Fostamatinib.
DrugCentral; Q04771; -.
GuidetoPHARMACOLOGY; 1785; -.
iPTMnet; Q04771; -.
PhosphoSitePlus; Q04771; -.
BioMuta; ACVR1; -.
DMDM; 462447; -.
EPD; Q04771; -.
jPOST; Q04771; -.
MassIVE; Q04771; -.
MaxQB; Q04771; -.
PaxDb; Q04771; -.
PeptideAtlas; Q04771; -.
PRIDE; Q04771; -.
ProteomicsDB; 58283; -.
Antibodypedia; 2371; 553 antibodies.
DNASU; 90; -.
Ensembl; ENST00000263640; ENSP00000263640; ENSG00000115170.
Ensembl; ENST00000409283; ENSP00000387273; ENSG00000115170.
Ensembl; ENST00000410057; ENSP00000387127; ENSG00000115170.
Ensembl; ENST00000424669; ENSP00000400767; ENSG00000115170.
Ensembl; ENST00000434821; ENSP00000405004; ENSG00000115170.
Ensembl; ENST00000539637; ENSP00000440091; ENSG00000115170.
Ensembl; ENST00000672582; ENSP00000500605; ENSG00000115170.
Ensembl; ENST00000673324; ENSP00000500109; ENSG00000115170.
GeneID; 90; -.
KEGG; hsa:90; -.
UCSC; uc002tzm.4; human.
CTD; 90; -.
DisGeNET; 90; -.
EuPathDB; HostDB:ENSG00000115170.13; -.
GeneCards; ACVR1; -.
HGNC; HGNC:171; ACVR1.
HPA; ENSG00000115170; Low tissue specificity.
MalaCards; ACVR1; -.
MIM; 102576; gene.
MIM; 135100; phenotype.
neXtProt; NX_Q04771; -.
OpenTargets; ENSG00000115170; -.
Orphanet; 337; Fibrodysplasia ossificans progressiva.
PharmGKB; PA24492; -.
eggNOG; KOG2052; Eukaryota.
eggNOG; ENOG410XQT0; LUCA.
GeneTree; ENSGT00940000160160; -.
HOGENOM; CLU_000288_8_5_1; -.
InParanoid; Q04771; -.
KO; K04675; -.
OMA; CQGQQCF; -.
OrthoDB; 1299087at2759; -.
PhylomeDB; Q04771; -.
TreeFam; TF314724; -.
BRENDA; 2.7.10.2; 2681.
SignaLink; Q04771; -.
SIGNOR; Q04771; -.
BioGRID-ORCS; 90; 4 hits in 816 CRISPR screens.
ChiTaRS; ACVR1; human.
EvolutionaryTrace; Q04771; -.
GeneWiki; ACVR1; -.
GenomeRNAi; 90; -.
Pharos; Q04771; Tchem.
PRO; PR:Q04771; -.
Proteomes; UP000005640; Chromosome 2.
RNAct; Q04771; protein.
Bgee; ENSG00000115170; Expressed in cartilage tissue and 233 other tissues.
ExpressionAtlas; Q04771; baseline and differential.
Genevisible; Q04771; HS.
GO; GO:0048179; C:activin receptor complex; IDA:UniProtKB.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0070724; C:BMP receptor complex; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0048185; F:activin binding; IDA:UniProtKB.
GO; GO:0016361; F:activin receptor activity, type I; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IDA:HGNC-UCL.
GO; GO:0045296; F:cadherin binding; IPI:ARUK-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0017046; F:peptide hormone binding; NAS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0004672; F:protein kinase activity; IDA:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:HGNC-UCL.
GO; GO:1990782; F:protein tyrosine kinase binding; IPI:ARUK-UCL.
GO; GO:0046332; F:SMAD binding; IDA:HGNC-UCL.
GO; GO:0050431; F:transforming growth factor beta binding; IDA:UniProtKB.
GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IBA:GO_Central.
GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; NAS:UniProtKB.
GO; GO:0032924; P:activin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
GO; GO:0003289; P:atrial septum primum morphogenesis; IMP:BHF-UCL.
GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
GO; GO:0061312; P:BMP signaling pathway involved in heart development; ISS:BHF-UCL.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
GO; GO:0060923; P:cardiac muscle cell fate commitment; IMP:BHF-UCL.
GO; GO:0071773; P:cellular response to BMP stimulus; IMP:BHF-UCL.
GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
GO; GO:0003143; P:embryonic heart tube morphogenesis; IMP:BHF-UCL.
GO; GO:0061445; P:endocardial cushion cell fate commitment; IMP:BHF-UCL.
GO; GO:0003274; P:endocardial cushion fusion; ISS:BHF-UCL.
GO; GO:0003203; P:endocardial cushion morphogenesis; ISS:BHF-UCL.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:HGNC-UCL.
GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
GO; GO:0007281; P:germ cell development; IEA:Ensembl.
GO; GO:0007507; P:heart development; IBA:GO_Central.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
GO; GO:0003183; P:mitral valve morphogenesis; IMP:BHF-UCL.
GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IMP:HGNC-UCL.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:BHF-UCL.
GO; GO:0009968; P:negative regulation of signal transduction; IMP:HGNC-UCL.
GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
GO; GO:0060037; P:pharyngeal system development; IEA:Ensembl.
GO; GO:0030501; P:positive regulation of bone mineralization; IMP:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IGI:BHF-UCL.
GO; GO:2000017; P:positive regulation of determination of dorsal identity; IDA:BHF-UCL.
GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:ARUK-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:HGNC-UCL.
GO; GO:0030278; P:regulation of ossification; IMP:UniProtKB.
GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
InterPro; IPR000472; Activin_recp.
InterPro; IPR003605; GS_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR000333; TGFB_receptor.
PANTHER; PTHR23255; PTHR23255; 1.
Pfam; PF01064; Activin_recp; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF08515; TGF_beta_GS; 1.
PRINTS; PR00653; ACTIVIN2R.
SMART; SM00467; GS; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51256; GS; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Disease mutation; Glycoprotein; Kinase;
Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
Transmembrane helix.
SIGNAL 1..20
/evidence="ECO:0000250"
CHAIN 21..509
/note="Activin receptor type-1"
/id="PRO_0000024394"
TOPO_DOM 21..123
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 124..146
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 147..509
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 178..207
/note="GS"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00585"
DOMAIN 208..502
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 214..222
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
ACT_SITE 336
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027"
BINDING 235
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 501
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19369195"
CARBOHYD 102
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
VARIANT 15
/note="A -> G (in dbSNP:rs13406336)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041392"
VARIANT 41
/note="S -> F (in dbSNP:rs55957214)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041393"
VARIANT 47
/note="H -> Q (in dbSNP:rs34056189)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041394"
VARIANT 115
/note="P -> S (in a melanoma sample; somatic mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041395"
VARIANT 197..198
/note="PF -> L (in FOP; variant phenotype)"
/evidence="ECO:0000269|PubMed:19085907"
/id="VAR_058418"
VARIANT 202
/note="R -> I (in FOP; with some atypical features;
dbSNP:rs387906591)"
/evidence="ECO:0000269|PubMed:19330033"
/id="VAR_058419"
VARIANT 206
/note="R -> H (in FOP; dbSNP:rs121912678)"
/evidence="ECO:0000269|PubMed:16642017,
ECO:0000269|PubMed:19085907"
/id="VAR_028444"
VARIANT 207
/note="Q -> E (in FOP; with some atypical features)"
/evidence="ECO:0000269|PubMed:19085907"
/id="VAR_058420"
VARIANT 328
/note="G -> E (in FOP; variant phenotype;
dbSNP:rs387906589)"
/evidence="ECO:0000269|PubMed:19085907,
ECO:0000269|PubMed:19330033"
/id="VAR_058421"
VARIANT 328
/note="G -> R (in FOP; variant phenotype;
dbSNP:rs387906588)"
/evidence="ECO:0000269|PubMed:19085907"
/id="VAR_058422"
VARIANT 328
/note="G -> W (in FOP; variant phenotype;
dbSNP:rs387906588)"
/evidence="ECO:0000269|PubMed:19085907"
/id="VAR_058423"
VARIANT 356
/note="G -> D (in FOP; variant phenotype;
dbSNP:rs121912679)"
/evidence="ECO:0000269|PubMed:19085907"
/id="VAR_058424"
VARIANT 375
/note="R -> P (in FOP; variant phenotype;
dbSNP:rs387906590)"
/evidence="ECO:0000269|PubMed:19085907"
/id="VAR_058425"
HELIX 180..184
/evidence="ECO:0000244|PDB:6I1S"
STRAND 194..196
/evidence="ECO:0000244|PDB:6I1S"
HELIX 198..205
/evidence="ECO:0000244|PDB:6I1S"
STRAND 209..217
/evidence="ECO:0000244|PDB:6SRH"
STRAND 220..227
/evidence="ECO:0000244|PDB:6SRH"
STRAND 230..237
/evidence="ECO:0000244|PDB:6SRH"
HELIX 239..241
/evidence="ECO:0000244|PDB:6SRH"
HELIX 242..254
/evidence="ECO:0000244|PDB:6SRH"
STRAND 265..272
/evidence="ECO:0000244|PDB:6SRH"
STRAND 274..283
/evidence="ECO:0000244|PDB:6SRH"
HELIX 291..297
/evidence="ECO:0000244|PDB:6SRH"
HELIX 302..320
/evidence="ECO:0000244|PDB:6SRH"
STRAND 325..327
/evidence="ECO:0000244|PDB:3MTF"
STRAND 331..333
/evidence="ECO:0000244|PDB:6SRH"
HELIX 339..341
/evidence="ECO:0000244|PDB:6SRH"
STRAND 342..344
/evidence="ECO:0000244|PDB:6SRH"
STRAND 350..352
/evidence="ECO:0000244|PDB:6SRH"
STRAND 359..361
/evidence="ECO:0000244|PDB:6SRH"
TURN 363..366
/evidence="ECO:0000244|PDB:6SRH"
STRAND 367..369
/evidence="ECO:0000244|PDB:6SRH"
HELIX 379..381
/evidence="ECO:0000244|PDB:6SRH"
HELIX 384..387
/evidence="ECO:0000244|PDB:6SRH"
HELIX 396..415
/evidence="ECO:0000244|PDB:6SRH"
TURN 430..434
/evidence="ECO:0000244|PDB:6SRH"
HELIX 441..448
/evidence="ECO:0000244|PDB:6SRH"
HELIX 459..463
/evidence="ECO:0000244|PDB:6SRH"
HELIX 465..477
/evidence="ECO:0000244|PDB:6SRH"
HELIX 482..484
/evidence="ECO:0000244|PDB:6SRH"
HELIX 488..496
/evidence="ECO:0000244|PDB:6SRH"
SEQUENCE 509 AA; 57153 MW; E2B0F051D19DD052 CRC64;
MVDGVMILPV LIMIALPSPS MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN
DGFHVYQKGC FQVYEQGKMT CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF
HLEVGLIILS VVFAVCLLAC LLGVALRKFK RRNQERLNPR DVEYGTIEGL ITTNVGDSTL
ADLLDHSCTS GSGSGLPFLV QRTVARQITL LECVGKGRYG EVWRGSWQGE NVAVKIFSSR
DEKSWFRETE LYNTVMLRHE NILGFIASDM TSRHSSTQLW LITHYHEMGS LYDYLQLTTL
DTVSCLRIVL SIASGLAHLH IEIFGTQGKP AIAHRDLKSK NILVKKNGQC CIADLGLAVM
HSQSTNQLDV GNNPRVGTKR YMAPEVLDET IQVDCFDSYK RVDIWAFGLV LWEVARRMVS
NGIVEDYKPP FYDVVPNDPS FEDMRKVVCV DQQRPNIPNR WFSDPTLTSL AKLMKECWYQ
NPSARLTALR IKKTLTKIDN SLDKLKTDC


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