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Serine/threonine-protein kinase receptor R3 (SKR3) (EC 2.7.11.30) (Activin receptor-like kinase 1) (ALK-1) (TGF-B superfamily receptor type I) (TSR-I)

 ACVL1_HUMAN             Reviewed;         503 AA.
P37023; A6NGA8;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
22-NOV-2017, entry version 195.
RecName: Full=Serine/threonine-protein kinase receptor R3;
Short=SKR3;
EC=2.7.11.30;
AltName: Full=Activin receptor-like kinase 1;
Short=ALK-1;
AltName: Full=TGF-B superfamily receptor type I;
Short=TSR-I;
Flags: Precursor;
Name=ACVRL1; Synonyms=ACVRLK1, ALK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8242742; DOI=10.1016/0092-8674(93)90488-C;
Attisano L., Carcamo J., Ventura F., Weis F.M., Massague J.,
Wrana J.L.;
"Identification of human activin and TGF beta type I receptors that
form heteromeric kinase complexes with type II receptors.";
Cell 75:671-680(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HHT2 CYS-50; GLN-67;
ILE-333; TRP-374 AND THR-424.
PubMed=9245985; DOI=10.1086/513903;
Berg J.N., Gallione C.J., Stenzel T.T., Johnson D.W., Allen W.P.,
Schwartz C.E., Jackson C.E., Porteous M.E.M., Marchuk D.A.;
"The activin receptor-like kinase 1 gene: genomic structure and
mutations in hereditary hemorrhagic telangiectasia type 2.";
Am. J. Hum. Genet. 61:60-67(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
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.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[7]
STRUCTURE BY NMR OF 19-118, FUNCTION AS BMP9 RECEPTOR, DISULFIDE
BONDS, AND MUTAGENESIS OF 74-ARG--LEU-76.
PubMed=22799562; DOI=10.1021/bi300942x;
Mahlawat P., Ilangovan U., Biswas T., Sun L.Z., Hinck A.P.;
"Structure of the Alk1 extracellular domain and characterization of
its bone morphogenetic protein (BMP) binding properties.";
Biochemistry 51:6328-6341(2012).
[8]
X-RAY CRYSTALLOGRAPHY (3.36 ANGSTROMS) OF 22-118 IN COMPLEX WITH BMP9
AND ACVR2B, FUNCTION AS BMP9 AND BMP10 RECEPTOR, AND DISULFIDE BONDS.
PubMed=22718755; DOI=10.1074/jbc.M112.377960;
Townson S.A., Martinez-Hackert E., Greppi C., Lowden P., Sako D.,
Liu J., Ucran J.A., Liharska K., Underwood K.W., Seehra J., Kumar R.,
Grinberg A.V.;
"Specificity and structure of a high affinity activin receptor-like
kinase 1 (ALK1) signaling complex.";
J. Biol. Chem. 287:27313-27325(2012).
[9]
VARIANTS HHT2 SER-232 DEL; ARG-376 AND GLN-411.
PubMed=8640225; DOI=10.1038/ng0696-189;
Johnson D.W., Berg J.N., Baldwin M.A., Gallione C.J., Marondel I.,
Yoon S.-J., Stenzel T.T., Speer M., Pericak-Vance M.A., Diamond A.,
Guttmacher A.E., Jackson C.E., Attisano L., Kucherlapati R.,
Porteous M.E.M., Marchuk D.A.;
"Mutations in the activin receptor-like kinase 1 gene in hereditary
haemorrhagic telangiectasia type 2.";
Nat. Genet. 13:189-194(1996).
[10]
VARIANTS HHT2 TYR-51; TRP-77 AND ASP-96.
PubMed=10694922;
DOI=10.1002/(SICI)1098-1004(1998)12:2<137::AID-HUMU15>3.0.CO;2-M;
Klaus D.J., Gallione C.J., Anthony K., Yeh E.Y., Yu J., Lux A.,
Johnson D.W., Marchuk D.A.;
"Novel missense and frameshift mutations in the activin receptor-like
kinase-1 gene in hereditary hemorrhagic telangiectasia.";
Hum. Mutat. 12:137-137(1998).
[11]
VARIANTS HHT2 GLY-48-49-ALA DELINS EP; CYS-50; SER-232 DEL; ILE-333;
TYR-344 AND ASP-407.
PubMed=10767348; DOI=10.1093/hmg/9.8.1227;
Abdalla S.A., Pece-Barbara N., Vera S., Tapia E., Paez E.,
Bernabeu C., Letarte M.;
"Analysis of ALK-1 and endoglin in newborns from families with
hereditary hemorrhagic telangiectasia type 2.";
Hum. Mol. Genet. 9:1227-1237(2000).
[12]
VARIANTS HHT2 TRP-374 AND ASN-398.
PubMed=11170071;
DOI=10.1002/1096-8628(20010201)98:4<298::AID-AJMG1093>3.0.CO;2-K;
Kjeldsen A.D., Brusgaard K., Poulsen L., Kruse T., Rasmussen K.,
Green A., Vase P.;
"Mutations in the ALK-1 gene and the phenotype of hereditary
hemorrhagic telangiectasia in two large Danish families.";
Am. J. Med. Genet. 98:298-302(2001).
[13]
VARIANTS HHT2 ASP-254 DEL; TRP-411 AND TRP-484.
PubMed=11484689; DOI=10.1056/NEJM200108023450503;
Trembath R.C., Thomson J.R., Machado R.D., Morgan N.V., Atkinson C.,
Winship I., Simonneau G., Galie N., Loyd J.E., Humbert M.,
Nichols W.C., Berg J., Manes A., McGaughran J., Pauciulo M.,
Wheeler L., Morrell N.W.;
"Clinical and molecular genetic features of pulmonary hypertension in
patients with hereditary hemorrhagic telangiectasia.";
N. Engl. J. Med. 345:325-334(2001).
[14]
VARIANTS HHT2 ALA-179; ASP-211; TYR-344; TRP-374; GLN-374; SER-399;
GLN-411 AND THR-487, AND CHARACTERIZATION OF VARIANTS HHT2 CYS-50;
GLN-67; TRP-77; ALA-179; ASP-211; SER-232 DEL; ASP-254 DEL; ILE-333;
TYR-344; GLN-374; LEU-378; GLN-411 AND THR-487.
PubMed=14684682; DOI=10.1136/jmg.40.12.865;
Harrison R.E., Flanagan J.A., Sankelo M., Abdalla S.A., Rowell J.,
Machado R.D., Elliott C.G., Robbins I.M., Olschewski H.,
McLaughlin V., Gruenig E., Kermeen F., Halme M.,
Raeisaenen-Sokolowski A., Laitinen T., Morrell N.W., Trembath R.C.;
"Molecular and functional analysis identifies ALK-1 as the predominant
cause of pulmonary hypertension related to hereditary haemorrhagic
telangiectasia.";
J. Med. Genet. 40:865-871(2003).
[15]
ERRATUM.
Harrison R.E., Flanagan J.A., Sankelo M., Abdalla S.A., Rowell J.,
Machado R.D., Elliott C.G., Robbins I.M., Olschewski H.,
McLaughlin V., Gruenig E., Kermeen F., Halme M.,
Raeisaenen-Sokolowski A., Laitinen T., Morrell N.W., Trembath R.C.;
J. Med. Genet. 41:576-576(2004).
[16]
VARIANTS HHT2 ARG-48; LYS-215; ARG-223; ARG-229; SER-233 DEL; PHE-285;
PRO-306; TYR-314; PRO-337; PRO-347; GLN-374; VAL-376; LYS-379;
GLY-397; TRP-411; PRO-411; GLN-411; LEU-425; LEU-479; VAL-482 AND
TRP-484.
PubMed=15024723; DOI=10.1002/humu.20017;
French Rendu-Osler network;
Lesca G., Plauchu H., Coulet F., Lefebvre S., Plessis G., Odent S.,
Riviere S., Leheup B., Goizet C., Carette M.-F., Cordier J.-F.,
Pinson S., Soubrier F., Calender A., Giraud S.;
"Molecular screening of ALK1/ACVRL1 and ENG genes in hereditary
hemorrhagic telangiectasia in France.";
Hum. Mutat. 23:289-299(2004).
[17]
VARIANTS HHT2 TRP-67; TRP-374; LYS-379; ASP-407; TRP-411; VAL-425 AND
PHE-425 DEL.
PubMed=15712270; DOI=10.1002/humu.9311;
Kuehl H.K.A., Caselitz M., Hasenkamp S., Wagner S., El-Harith E.-H.A.,
Manns M.P., Stuhrmann M.;
"Hepatic manifestation is associated with ALK1 in hereditary
hemorrhagic telangiectasia: identification of five novel ALK1 and one
novel ENG mutations.";
Hum. Mutat. 25:320-320(2005).
[18]
VARIANT SER-30, AND VARIANTS HHT2 TYR-34; ALA-52; ILE-197; ASP-219;
LYS-237; LEU-260; PRO-289; ARG-344; CYS-426 AND ARG-433.
PubMed=16752392; DOI=10.1002/humu.20342;
Bossler A.D., Richards J., George C., Godmilow L., Ganguly A.;
"Novel mutations in ENG and ACVRL1 identified in a series of 200
individuals undergoing clinical genetic testing for hereditary
hemorrhagic telangiectasia (HHT): correlation of genotype with
phenotype.";
Hum. Mutat. 27:667-675(2006).
[19]
VARIANTS HHT2 GLY-50; PRO-66; ARG-69; TYR-176; LEU-233; PRO-265;
PRO-403 AND SER-416.
PubMed=16525724;
Argyriou L., Twelkemeyer S., Panchulidze I., Wehner L.E., Teske U.,
Engel W., Nayernia K.;
"Novel mutations in the ENG and ACVRL1 genes causing hereditary
hemorrhagic teleangiectasia.";
Int. J. Mol. Med. 17:655-659(2006).
[20]
VARIANTS CYS-38; PRO-138; LYS-277; PRO-342; THR-400 AND GLU-486, AND
VARIANTS HHT2 SER-96; GLY-217; GLU-226; ARG-280; ARG-294; GLN-328;
HIS-335; ASP-347; SER-378; ARG-424; SER-449 AND PRO-479.
PubMed=20414677; DOI=10.1007/s00439-010-0825-4;
Richards-Yutz J., Grant K., Chao E.C., Walther S.E., Ganguly A.;
"Update on molecular diagnosis of hereditary hemorrhagic
telangiectasia.";
Hum. Genet. 128:61-77(2010).
[21]
VARIANTS ASN-8; VAL-59; VAL-159; CYS-225 AND ALA-396.
PubMed=24936649; DOI=10.1371/journal.pone.0100261;
Pousada G., Baloira A., Vilarino C., Cifrian J.M., Valverde D.;
"Novel mutations in BMPR2, ACVRL1 and KCNA5 genes and hemodynamic
parameters in patients with pulmonary arterial hypertension.";
PLoS ONE 9:E100261-E100261(2014).
[22]
VARIANTS HHT2 GLY-41; TYR-41; GLY-46; PRO-47; TYR-66; PHE-77; ASP-211;
SER-211; VAL-245; PRO-306; VAL-313; TYR-314; SER-378; ASP-379;
LYS-379; GLY-404; TRP-411; MET-441 AND TYR-443, VARIANTS ASP-111 AND
PHE-417, CHARACTERIZATION OF VARIANTS HHT2 GLY-41; TYR-41; GLY-46;
PRO-47; TYR-66; PHE-77; ASP-211; SER-211; VAL-245; PRO-306; VAL-313;
TYR-314; SER-378; ASP-379; LYS-379; GLY-404; TRP-411; MET-441 AND
TYR-443, CHARACTERIZATION OF VARIANTS ASP-111 AND PHE-417, FUNCTION,
AND SUBCELLULAR LOCATION.
PubMed=26176610; DOI=10.1371/journal.pone.0132111;
Alaa El Din F., Patri S., Thoreau V., Rodriguez-Ballesteros M.,
Hamade E., Bailly S., Gilbert-Dussardier B., Abou Merhi R., Kitzis A.;
"Functional and splicing defect analysis of 23 ACVRL1 mutations in a
cohort of patients affected by hereditary hemorrhagic
telangiectasia.";
PLoS ONE 10:E0132111-E0132111(2015).
-!- FUNCTION: Type I receptor for TGF-beta family ligands BMP9/GDF2
and BMP10 and important regulator of normal blood vessel
development. 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. May bind activin as
well. {ECO:0000269|PubMed:22718755, ECO:0000269|PubMed:22799562,
ECO:0000269|PubMed:26176610}.
-!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
protein] phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- INTERACTION:
P02750:LRG1; NbExp=3; IntAct=EBI-8043559, EBI-9083443;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26176610};
Single-pass type I membrane protein {ECO:0000255}.
-!- DISEASE: Telangiectasia, hereditary hemorrhagic, 2 (HHT2)
[MIM:600376]: A multisystemic vascular dysplasia leading to
dilation of permanent blood vessels and arteriovenous
malformations of skin, mucosa, and viscera. The disease is
characterized by recurrent epistaxis and gastro-intestinal
hemorrhage. Visceral involvement includes arteriovenous
malformations of the lung, liver, and brain.
{ECO:0000269|PubMed:10694922, ECO:0000269|PubMed:10767348,
ECO:0000269|PubMed:11170071, ECO:0000269|PubMed:11484689,
ECO:0000269|PubMed:14684682, ECO:0000269|PubMed:15024723,
ECO:0000269|PubMed:15712270, ECO:0000269|PubMed:16525724,
ECO:0000269|PubMed:16752392, ECO:0000269|PubMed:20414677,
ECO:0000269|PubMed:26176610, ECO:0000269|PubMed:8640225,
ECO:0000269|PubMed:9245985}. 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}.
-!- WEB RESOURCE: Name=Hereditary Hemorrhagic Telangiectasia and ENG;
URL="http://arup.utah.edu/database/ACVRL1/ACVRL1_welcome.php";
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EMBL; Z22533; CAA80255.1; -; mRNA.
EMBL; L17075; AAA16160.1; -; mRNA.
EMBL; U77713; AAB61900.1; -; Genomic_DNA.
EMBL; U77707; AAB61900.1; JOINED; Genomic_DNA.
EMBL; U77708; AAB61900.1; JOINED; Genomic_DNA.
EMBL; U77709; AAB61900.1; JOINED; Genomic_DNA.
EMBL; U77710; AAB61900.1; JOINED; Genomic_DNA.
EMBL; U77711; AAB61900.1; JOINED; Genomic_DNA.
EMBL; U77712; AAB61900.1; JOINED; Genomic_DNA.
EMBL; AC025259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471111; EAW58213.1; -; Genomic_DNA.
EMBL; BC042637; AAH42637.1; -; mRNA.
CCDS; CCDS31804.1; -.
PIR; A49431; A49431.
RefSeq; NP_000011.2; NM_000020.2.
RefSeq; NP_001070869.1; NM_001077401.1.
RefSeq; XP_005269292.1; XM_005269235.2.
UniGene; Hs.591026; -.
PDB; 2LCR; NMR; -; A=22-118.
PDB; 3MY0; X-ray; 2.65 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=195-497.
PDB; 4FAO; X-ray; 3.36 A; C/D/I/J/O/P/U/V/c/d/i/j=22-118.
PDBsum; 2LCR; -.
PDBsum; 3MY0; -.
PDBsum; 4FAO; -.
ProteinModelPortal; P37023; -.
SMR; P37023; -.
BioGrid; 106609; 19.
DIP; DIP-5938N; -.
IntAct; P37023; 4.
STRING; 9606.ENSP00000373574; -.
BindingDB; P37023; -.
ChEMBL; CHEMBL5311; -.
DrugBank; DB00171; Adenosine triphosphate.
GuidetoPHARMACOLOGY; 1784; -.
iPTMnet; P37023; -.
PhosphoSitePlus; P37023; -.
BioMuta; ACVRL1; -.
DMDM; 3915750; -.
EPD; P37023; -.
PaxDb; P37023; -.
PeptideAtlas; P37023; -.
PRIDE; P37023; -.
DNASU; 94; -.
Ensembl; ENST00000388922; ENSP00000373574; ENSG00000139567.
GeneID; 94; -.
KEGG; hsa:94; -.
UCSC; uc001rzj.4; human.
CTD; 94; -.
DisGeNET; 94; -.
EuPathDB; HostDB:ENSG00000139567.12; -.
GeneCards; ACVRL1; -.
GeneReviews; ACVRL1; -.
HGNC; HGNC:175; ACVRL1.
HPA; HPA007041; -.
MalaCards; ACVRL1; -.
MIM; 600376; phenotype.
MIM; 601284; gene.
neXtProt; NX_P37023; -.
OpenTargets; ENSG00000139567; -.
Orphanet; 774; Hereditary hemorrhagic telangiectasia.
Orphanet; 275777; Heritable pulmonary arterial hypertension.
PharmGKB; PA24496; -.
eggNOG; KOG2052; Eukaryota.
eggNOG; ENOG410XQT0; LUCA.
GeneTree; ENSGT00760000118876; -.
HOGENOM; HOG000230587; -.
HOVERGEN; HBG054502; -.
InParanoid; P37023; -.
KO; K13594; -.
PhylomeDB; P37023; -.
TreeFam; TF314724; -.
BRENDA; 2.7.10.2; 2681.
BRENDA; 2.7.11.30; 2681.
Reactome; R-HSA-201451; Signaling by BMP.
SignaLink; P37023; -.
SIGNOR; P37023; -.
ChiTaRS; ACVRL1; human.
GeneWiki; ACVRL1; -.
GenomeRNAi; 94; -.
PRO; PR:P37023; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000139567; -.
CleanEx; HS_ACVRL1; -.
ExpressionAtlas; P37023; baseline and differential.
Genevisible; P37023; HS.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0048185; F:activin binding; IDA:UniProtKB.
GO; GO:0016361; F:activin receptor activity, type I; IDA:MGI.
GO; GO:0005524; F:ATP binding; IDA:HGNC.
GO; GO:0098821; F:BMP receptor activity; IMP:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:HGNC.
GO; GO:0004702; F:signal transducer, downstream of receptor, with serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0046332; F:SMAD binding; IDA:HGNC.
GO; GO:0050431; F:transforming growth factor beta binding; IPI:UniProtKB.
GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IEA:Ensembl.
GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IDA:MGI.
GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; NAS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IMP:HGNC.
GO; GO:0060840; P:artery development; ISS:BHF-UCL.
GO; GO:0008015; P:blood circulation; IMP:HGNC.
GO; GO:0002043; P:blood vessel endothelial cell proliferation involved in sprouting angiogenesis; TAS:DFLAT.
GO; GO:0001955; P:blood vessel maturation; TAS:DFLAT.
GO; GO:0001974; P:blood vessel remodeling; ISS:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; IMP:BHF-UCL.
GO; GO:0071773; P:cellular response to BMP stimulus; IMP:BHF-UCL.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:BHF-UCL.
GO; GO:0035912; P:dorsal aorta morphogenesis; ISS:BHF-UCL.
GO; GO:0003203; P:endocardial cushion morphogenesis; ISS:BHF-UCL.
GO; GO:0061154; P:endothelial tube morphogenesis; IMP:BHF-UCL.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0001946; P:lymphangiogenesis; ISS:BHF-UCL.
GO; GO:0060836; P:lymphatic endothelial cell differentiation; IMP:BHF-UCL.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IMP:BHF-UCL.
GO; GO:0007162; P:negative regulation of cell adhesion; IMP:HGNC.
GO; GO:0030308; P:negative regulation of cell growth; IDA:BHF-UCL.
GO; GO:0030336; P:negative regulation of cell migration; IMP:HGNC.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:HGNC.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IMP:BHF-UCL.
GO; GO:0045602; P:negative regulation of endothelial cell differentiation; IEA:Ensembl.
GO; GO:0010596; P:negative regulation of endothelial cell migration; IDA:BHF-UCL.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:HGNC.
GO; GO:0010629; P:negative regulation of gene expression; ISS:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IDA:BHF-UCL.
GO; GO:0032332; P:positive regulation of chondrocyte differentiation; TAS:BHF-UCL.
GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IEA:Ensembl.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:HGNC.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:HGNC.
GO; GO:0008217; P:regulation of blood pressure; IMP:HGNC.
GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; TAS:DFLAT.
GO; GO:0006275; P:regulation of DNA replication; TAS:DFLAT.
GO; GO:0001936; P:regulation of endothelial cell proliferation; TAS:DFLAT.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:HGNC.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:BHF-UCL.
GO; GO:0007165; P:signal transduction; IDA:HGNC.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:HGNC.
GO; GO:0060841; P:venous blood vessel development; ISS:BHF-UCL.
GO; GO:0035313; P:wound healing, spreading of epidermal cells; IMP:HGNC.
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; PF07714; Pkinase_Tyr; 1.
Pfam; PF08515; TGF_beta_GS; 1.
PRINTS; PR00653; ACTIVIN2R.
SMART; SM00467; GS; 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; Angiogenesis; ATP-binding; Cell membrane;
Complete proteome; Disease mutation; Disulfide bond; 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 21 {ECO:0000255}.
CHAIN 22 503 Serine/threonine-protein kinase receptor
R3.
/FTId=PRO_0000024420.
TOPO_DOM 22 118 Extracellular. {ECO:0000255}.
TRANSMEM 119 141 Helical. {ECO:0000255}.
TOPO_DOM 142 503 Cytoplasmic. {ECO:0000255}.
DOMAIN 172 201 GS. {ECO:0000255|PROSITE-
ProRule:PRU00585}.
DOMAIN 202 492 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 208 216 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 73 76 Mediates specificity for BMP ligand.
ACT_SITE 330 330 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 229 229 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000250|UniProtKB:Q61288}.
MOD_RES 160 160 Phosphoserine.
{ECO:0000250|UniProtKB:Q61288}.
MOD_RES 161 161 Phosphoserine.
{ECO:0000250|UniProtKB:Q61288}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 34 51 {ECO:0000244|PDB:2LCR,
ECO:0000244|PDB:4FAO,
ECO:0000269|PubMed:22718755,
ECO:0000269|PubMed:22799562}.
DISULFID 36 41 {ECO:0000244|PDB:2LCR,
ECO:0000244|PDB:4FAO,
ECO:0000269|PubMed:22718755,
ECO:0000269|PubMed:22799562}.
DISULFID 46 69 {ECO:0000244|PDB:2LCR,
ECO:0000244|PDB:4FAO,
ECO:0000269|PubMed:22718755,
ECO:0000269|PubMed:22799562}.
DISULFID 77 89 {ECO:0000244|PDB:2LCR,
ECO:0000244|PDB:4FAO,
ECO:0000269|PubMed:22718755,
ECO:0000269|PubMed:22799562}.
DISULFID 90 95 {ECO:0000244|PDB:2LCR,
ECO:0000244|PDB:4FAO,
ECO:0000269|PubMed:22718755,
ECO:0000269|PubMed:22799562}.
VARIANT 8 8 K -> N. {ECO:0000269|PubMed:24936649}.
/FTId=VAR_079583.
VARIANT 30 30 P -> S (found in a patient with
hereditary hemorrhagic talagiectasia;
unknown pathological significance;
dbSNP:rs149664056).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070308.
VARIANT 34 34 C -> Y (in HHT2).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070309.
VARIANT 38 38 S -> C. {ECO:0000269|PubMed:20414677}.
/FTId=VAR_070310.
VARIANT 41 41 C -> G (in HHT2; loss of receptor
activity in response to BMP9;
predominantly retained in the endoplasmic
reticulum).
{ECO:0000269|PubMed:26176610}.
/FTId=VAR_075231.
VARIANT 41 41 C -> Y (in HHT2; loss of receptor
activity in response to BMP9;
predominantly retained in the endoplasmic
reticulum).
{ECO:0000269|PubMed:26176610}.
/FTId=VAR_075232.
VARIANT 46 46 C -> G (in HHT2; loss of receptor
activity in response to BMP9; retained in
the endoplasmic reticulum).
{ECO:0000269|PubMed:26176610}.
/FTId=VAR_075233.
VARIANT 47 47 R -> P (in HHT2; loss of receptor
activity in response to BMP9; retained in
the endoplasmic reticulum).
{ECO:0000269|PubMed:26176610}.
/FTId=VAR_075234.
VARIANT 48 49 GA -> EP (in HHT2; dbSNP:rs387906392).
/FTId=VAR_026784.
VARIANT 48 48 G -> R (in HHT2).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026785.
VARIANT 50 50 W -> C (in HHT2; retained in the
endoplasmic reticulum;
dbSNP:rs121909285).
{ECO:0000269|PubMed:10767348,
ECO:0000269|PubMed:14684682,
ECO:0000269|PubMed:9245985}.
/FTId=VAR_006204.
VARIANT 50 50 W -> G (in HHT2).
{ECO:0000269|PubMed:16525724}.
/FTId=VAR_070311.
VARIANT 51 51 C -> Y (in HHT2; dbSNP:rs863223409).
{ECO:0000269|PubMed:10694922}.
/FTId=VAR_006205.
VARIANT 52 52 T -> A (in HHT2).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070312.
VARIANT 59 59 E -> V (found in a patient with pulmonary
arterial hypertension; unknown
pathological significance).
{ECO:0000269|PubMed:24936649}.
/FTId=VAR_079584.
VARIANT 66 66 H -> P (in HHT2).
{ECO:0000269|PubMed:16525724}.
/FTId=VAR_070313.
VARIANT 66 66 H -> Y (in HHT2; loss of receptor
activity in response to BMP9; retained in
the endoplasmic reticulum).
{ECO:0000269|PubMed:26176610}.
/FTId=VAR_075235.
VARIANT 67 67 R -> Q (in HHT2; retained in the
endoplasmic reticulum;
dbSNP:rs863223414).
{ECO:0000269|PubMed:14684682,
ECO:0000269|PubMed:9245985}.
/FTId=VAR_006206.
VARIANT 67 67 R -> W (in HHT2).
{ECO:0000269|PubMed:15712270}.
/FTId=VAR_026786.
VARIANT 69 69 C -> R (in HHT2).
{ECO:0000269|PubMed:16525724}.
/FTId=VAR_070314.
VARIANT 77 77 C -> F (in HHT2; loss of receptor
activity in response to BMP9; retained in
the endoplasmic reticulum).
{ECO:0000269|PubMed:26176610}.
/FTId=VAR_075236.
VARIANT 77 77 C -> W (in HHT2; retained in the
endoplasmic reticulum).
{ECO:0000269|PubMed:10694922,
ECO:0000269|PubMed:14684682}.
/FTId=VAR_006207.
VARIANT 96 96 N -> D (in HHT2).
{ECO:0000269|PubMed:10694922}.
/FTId=VAR_006208.
VARIANT 96 96 N -> S (in HHT2).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070315.
VARIANT 111 111 E -> D (rare polymorphism; no loss of
receptor activity in response to BMP9;
mutant protein is capable of targeting
the cell surface appropriately).
{ECO:0000269|PubMed:26176610}.
/FTId=VAR_075237.
VARIANT 138 138 L -> P. {ECO:0000269|PubMed:20414677}.
/FTId=VAR_070316.
VARIANT 159 159 E -> V (found in a patient with pulmonary
arterial hypertension; unknown
pathological significance).
{ECO:0000269|PubMed:24936649}.
/FTId=VAR_079585.
VARIANT 176 176 D -> Y (in HHT2).
{ECO:0000269|PubMed:16525724}.
/FTId=VAR_070317.
VARIANT 179 179 D -> A (in HHT2; mutant protein is
capable of targeting the cell surface
appropriately; dbSNP:rs753792569).
{ECO:0000269|PubMed:14684682}.
/FTId=VAR_026787.
VARIANT 197 197 T -> I (in HHT2).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070318.
VARIANT 211 211 G -> D (in HHT2; loss of receptor
activity in response to BMP9; retained in
the endoplasmic reticulum;
dbSNP:rs28936687).
{ECO:0000269|PubMed:14684682,
ECO:0000269|PubMed:26176610}.
/FTId=VAR_026788.
VARIANT 211 211 G -> S (in HHT2; loss of receptor
activity in response to BMP9; retained in
the endoplasmic reticulum).
{ECO:0000269|PubMed:26176610}.
/FTId=VAR_075238.
VARIANT 215 215 E -> K (in HHT2; dbSNP:rs754283265).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026789.
VARIANT 217 217 W -> G (in HHT2).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070319.
VARIANT 219 219 G -> D (in HHT2).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070320.
VARIANT 223 223 G -> R (in HHT2).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026790.
VARIANT 225 225 S -> C (found in a patient with pulmonary
arterial hypertension; unknown
pathological significance).
{ECO:0000269|PubMed:24936649}.
/FTId=VAR_079586.
VARIANT 226 226 V -> E (in HHT2).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070321.
VARIANT 229 229 K -> R (in HHT2).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026791.
VARIANT 232 232 Missing (in HHT2; mutant protein is
capable of targeting the cell surface
appropriately).
{ECO:0000269|PubMed:10767348,
ECO:0000269|PubMed:14684682,
ECO:0000269|PubMed:8640225}.
/FTId=VAR_006209.
VARIANT 233 233 S -> L (in HHT2; dbSNP:rs762773076).
{ECO:0000269|PubMed:16525724}.
/FTId=VAR_070322.
VARIANT 233 233 Missing (in HHT2).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026792.
VARIANT 237 237 Q -> K (in HHT2).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070323.
VARIANT 245 245 I -> N (in dbSNP:rs1804508).
/FTId=VAR_011717.
VARIANT 245 245 I -> V (in HHT2; no loss of receptor
activity in response to BMP9; mutant
protein is capable of targeting the cell
surface appropriately; affects splicing
by inducing the creation of a new donor
splice site and the loss of the 3' end of
exon 6). {ECO:0000269|PubMed:26176610}.
/FTId=VAR_075239.
VARIANT 254 254 Missing (in HHT2; retained in the
endoplasmic reticulum).
{ECO:0000269|PubMed:11484689,
ECO:0000269|PubMed:14684682}.
/FTId=VAR_026793.
VARIANT 260 260 I -> L (in HHT2).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070324.
VARIANT 265 265 T -> P (in HHT2).
{ECO:0000269|PubMed:16525724}.
/FTId=VAR_070325.
VARIANT 277 277 T -> K (found in a patient with
hereditary hemorrhagic talagiectasia;
unknown pathological significance).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070326.
VARIANT 280 280 H -> R (in HHT2).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070327.
VARIANT 285 285 L -> F (in HHT2).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026794.
VARIANT 289 289 L -> P (in HHT2).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070328.
VARIANT 294 294 L -> R (in HHT2).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070329.
VARIANT 306 306 A -> P (in HHT2; loss of receptor
activity in response to BMP9; retained in
the endoplasmic reticulum).
{ECO:0000269|PubMed:15024723,
ECO:0000269|PubMed:26176610}.
/FTId=VAR_026795.
VARIANT 313 313 L -> V (in HHT2; loss of receptor
activity in response to BMP9;
predominantly retained in the endoplasmic
reticulum).
{ECO:0000269|PubMed:26176610}.
/FTId=VAR_075240.
VARIANT 314 314 H -> Y (in HHT2; loss of receptor
activity in response to BMP9; retained in
the endoplasmic reticulum).
{ECO:0000269|PubMed:15024723,
ECO:0000269|PubMed:26176610}.
/FTId=VAR_026796.
VARIANT 328 328 H -> Q (in HHT2).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070330.
VARIANT 333 333 S -> I (in HHT2; retained in the
endoplasmic reticulum;
dbSNP:rs863223413).
{ECO:0000269|PubMed:10767348,
ECO:0000269|PubMed:14684682,
ECO:0000269|PubMed:9245985}.
/FTId=VAR_006210.
VARIANT 335 335 N -> H (in HHT2).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070331.
VARIANT 337 337 L -> P (in HHT2).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026797.
VARIANT 342 342 L -> P. {ECO:0000269|PubMed:20414677}.
/FTId=VAR_070332.
VARIANT 344 344 C -> R (in HHT2).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070333.
VARIANT 344 344 C -> Y (in HHT2; retained in the
endoplasmic reticulum; dbSNP:rs28936688).
{ECO:0000269|PubMed:10767348,
ECO:0000269|PubMed:14684682}.
/FTId=VAR_026798.
VARIANT 347 347 A -> D (in HHT2).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070334.
VARIANT 347 347 A -> P (in HHT2).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026799.
VARIANT 374 374 R -> Q (in HHT2; retained in the
endoplasmic reticulum).
{ECO:0000269|PubMed:14684682,
ECO:0000269|PubMed:15024723}.
/FTId=VAR_026800.
VARIANT 374 374 R -> W (in HHT2; dbSNP:rs28936401).
{ECO:0000269|PubMed:11170071,
ECO:0000269|PubMed:14684682,
ECO:0000269|PubMed:15712270,
ECO:0000269|PubMed:9245985}.
/FTId=VAR_006211.
VARIANT 376 376 M -> R (in HHT2; dbSNP:rs28936399).
{ECO:0000269|PubMed:8640225}.
/FTId=VAR_006212.
VARIANT 376 376 M -> V (in HHT2).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026801.
VARIANT 378 378 P -> L (in HHT2; retained in the
endoplasmic reticulum).
{ECO:0000269|PubMed:14684682}.
/FTId=VAR_026802.
VARIANT 378 378 P -> S (in HHT2; loss of receptor
activity in response to BMP9; retained in
the endoplasmic reticulum).
{ECO:0000269|PubMed:20414677,
ECO:0000269|PubMed:26176610}.
/FTId=VAR_070335.
VARIANT 379 379 E -> D (in HHT2; loss of receptor
activity in response to BMP9; retained in
the endoplasmic reticulum).
{ECO:0000269|PubMed:26176610}.
/FTId=VAR_075241.
VARIANT 379 379 E -> K (in HHT2; loss of receptor
activity in response to BMP9; retained in
the endoplasmic reticulum).
{ECO:0000269|PubMed:15024723,
ECO:0000269|PubMed:15712270,
ECO:0000269|PubMed:26176610}.
/FTId=VAR_026803.
VARIANT 396 396 T -> A (found in patients with pulmonary
arterial hypertension; unknown
pathological significance).
{ECO:0000269|PubMed:24936649}.
/FTId=VAR_079587.
VARIANT 397 397 D -> G (in HHT2).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026804.
VARIANT 398 398 I -> N (in HHT2; dbSNP:rs121909286).
{ECO:0000269|PubMed:11170071}.
/FTId=VAR_026805.
VARIANT 399 399 W -> S (in HHT2; dbSNP:rs121909289).
{ECO:0000269|PubMed:14684682}.
/FTId=VAR_026806.
VARIANT 400 400 A -> T (found in a patient with
hereditary hemorrhagic talagiectasia;
unknown pathological significance).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070336.
VARIANT 403 403 L -> P (in HHT2).
{ECO:0000269|PubMed:16525724}.
/FTId=VAR_070337.
VARIANT 404 404 V -> G (in HHT2; loss of receptor
activity in response to BMP9;
predominantly retained in the endoplasmic
reticulum).
{ECO:0000269|PubMed:26176610}.
/FTId=VAR_075242.
VARIANT 407 407 E -> D (in HHT2).
{ECO:0000269|PubMed:10767348,
ECO:0000269|PubMed:15712270}.
/FTId=VAR_026807.
VARIANT 411 411 R -> P (in HHT2; dbSNP:rs121909284).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026808.
VARIANT 411 411 R -> Q (in HHT2; retained in the
endoplasmic reticulum;
dbSNP:rs121909284).
{ECO:0000269|PubMed:14684682,
ECO:0000269|PubMed:15024723,
ECO:0000269|PubMed:8640225}.
/FTId=VAR_006213.
VARIANT 411 411 R -> W (in HHT2; loss of receptor
activity in response to BMP9;
predominantly retained in the endoplasmic
reticulum; dbSNP:rs121909287).
{ECO:0000269|PubMed:11484689,
ECO:0000269|PubMed:15024723,
ECO:0000269|PubMed:15712270,
ECO:0000269|PubMed:26176610}.
/FTId=VAR_026809.
VARIANT 416 416 G -> S (in HHT2).
{ECO:0000269|PubMed:16525724}.
/FTId=VAR_070338.
VARIANT 417 417 I -> F (rare polymorphism; no loss of
receptor activity in response to BMP9;
mutant protein is capable of targeting
the cell surface appropriately;
dbSNP:rs141653630).
{ECO:0000269|PubMed:26176610}.
/FTId=VAR_075243.
VARIANT 424 424 P -> R (in HHT2).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070339.
VARIANT 424 424 P -> T (in HHT2).
{ECO:0000269|PubMed:9245985}.
/FTId=VAR_006214.
VARIANT 425 425 F -> L (in HHT2).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026810.
VARIANT 425 425 F -> V (in HHT2).
{ECO:0000269|PubMed:15712270}.
/FTId=VAR_026811.
VARIANT 425 425 Missing (in HHT2).
{ECO:0000269|PubMed:15712270}.
/FTId=VAR_026812.
VARIANT 426 426 Y -> C (in HHT2).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070340.
VARIANT 433 433 P -> R (in HHT2).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070341.
VARIANT 441 441 V -> M (in HHT2; retained in the
endoplasmic reticulum).
{ECO:0000269|PubMed:26176610}.
/FTId=VAR_075244.
VARIANT 443 443 C -> Y (in HHT2; retained in the
endoplasmic reticulum).
{ECO:0000269|PubMed:26176610}.
/FTId=VAR_075245.
VARIANT 449 449 P -> S (in HHT2).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070342.
VARIANT 479 479 R -> L (in HHT2).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026813.
VARIANT 479 479 R -> P (in HHT2).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070343.
VARIANT 482 482 A -> V (in HHT2; dbSNP:rs139142865).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026814.
VARIANT 484 484 R -> W (in HHT2; dbSNP:rs121909288).
{ECO:0000269|PubMed:11484689,
ECO:0000269|PubMed:15024723}.
/FTId=VAR_026815.
VARIANT 486 486 K -> E (found in a patient with
hereditary hemorrhagic talagiectasia;
unknown pathological significance;
dbSNP:rs113700354).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070344.
VARIANT 487 487 K -> T (in HHT2; mutant protein is
capable of targeting the cell surface
appropriately).
{ECO:0000269|PubMed:14684682}.
/FTId=VAR_026816.
MUTAGEN 74 76 REL->DFQ: Affinity for BMP9 decreased by
200-fold. {ECO:0000269|PubMed:22799562}.
CONFLICT 172 172 S -> T (in Ref. 1; CAA80255).
{ECO:0000305}.
HELIX 26 28 {ECO:0000244|PDB:2LCR}.
STRAND 32 35 {ECO:0000244|PDB:4FAO}.
STRAND 42 56 {ECO:0000244|PDB:4FAO}.
STRAND 59 61 {ECO:0000244|PDB:4FAO}.
STRAND 64 68 {ECO:0000244|PDB:4FAO}.
HELIX 74 78 {ECO:0000244|PDB:4FAO}.
STRAND 83 90 {ECO:0000244|PDB:4FAO}.
TURN 93 96 {ECO:0000244|PDB:4FAO}.
HELIX 198 201 {ECO:0000244|PDB:3MY0}.
STRAND 203 211 {ECO:0000244|PDB:3MY0}.
STRAND 214 221 {ECO:0000244|PDB:3MY0}.
STRAND 224 231 {ECO:0000244|PDB:3MY0}.
HELIX 233 235 {ECO:0000244|PDB:3MY0}.
HELIX 236 248 {ECO:0000244|PDB:3MY0}.
STRAND 259 265 {ECO:0000244|PDB:3MY0}.
STRAND 267 269 {ECO:0000244|PDB:3MY0}.
STRAND 272 278 {ECO:0000244|PDB:3MY0}.
HELIX 285 291 {ECO:0000244|PDB:3MY0}.
HELIX 296 314 {ECO:0000244|PDB:3MY0}.
STRAND 325 327 {ECO:0000244|PDB:3MY0}.
STRAND 335 338 {ECO:0000244|PDB:3MY0}.
STRAND 344 346 {ECO:0000244|PDB:3MY0}.
STRAND 353 355 {ECO:0000244|PDB:3MY0}.
STRAND 357 359 {ECO:0000244|PDB:3MY0}.
HELIX 373 375 {ECO:0000244|PDB:3MY0}.
HELIX 378 381 {ECO:0000244|PDB:3MY0}.
HELIX 390 410 {ECO:0000244|PDB:3MY0}.
TURN 424 428 {ECO:0000244|PDB:3MY0}.
HELIX 435 442 {ECO:0000244|PDB:3MY0}.
STRAND 455 459 {ECO:0000244|PDB:3MY0}.
TURN 460 462 {ECO:0000244|PDB:3MY0}.
HELIX 463 469 {ECO:0000244|PDB:3MY0}.
HELIX 476 478 {ECO:0000244|PDB:3MY0}.
HELIX 482 491 {ECO:0000244|PDB:3MY0}.
SEQUENCE 503 AA; 56124 MW; 074522AA802325DD CRC64;
MTLGSPRKGL LMLLMALVTQ GDPVKPSRGP LVTCTCESPH CKGPTCRGAW CTVVLVREEG
RHPQEHRGCG NLHRELCRGR PTEFVNHYCC DSHLCNHNVS LVLEATQPPS EQPGTDGQLA
LILGPVLALL ALVALGVLGL WHVRRRQEKQ RGLHSELGES SLILKASEQG DSMLGDLLDS
DCTTGSGSGL PFLVQRTVAR QVALVECVGK GRYGEVWRGL WHGESVAVKI FSSRDEQSWF
RETEIYNTVL LRHDNILGFI ASDMTSRNSS TQLWLITHYH EHGSLYDFLQ RQTLEPHLAL
RLAVSAACGL AHLHVEIFGT QGKPAIAHRD FKSRNVLVKS NLQCCIADLG LAVMHSQGSD
YLDIGNNPRV GTKRYMAPEV LDEQIRTDCF ESYKWTDIWA FGLVLWEIAR RTIVNGIVED
YRPPFYDVVP NDPSFEDMKK VVCVDQQTPT IPNRLAADPV LSGLAQMMRE CWYPNPSARL
TALRIKKTLQ KISNSPEKPK VIQ


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