Reviewed, UniProtKB/Swiss-Prot P37023 (ACVL1_HUMAN)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase receptor R3
      Short name=SKR3
    EC=2.7.11.30
Alternative name(s):
    Activin receptor-like kinase 1
      Short name=ALK-1
    TGF-B superfamily receptor type I
      Short name=TSR-I

Gene names

Name:	ACVRL1
Synonyms:	ACVRLK1, ALK1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

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 TGF-beta. May bind activin as well.
Catalytic activity	ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
Cofactor	Magnesium or manganese By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein.
Involvement in disease	Defects in ACVRL1 are the cause of hereditary hemorrhagic telangiectasia type 2 (HHT2) [MIM:600376]; also known as Osler-Rendu-Weber syndrome 2 (ORW2). HHT2 is an autosomal dominant multisystemic vascular dysplasia, characterized by recurrent epistaxis, muco-cutaneous telangiectases, gastro-intestinal hemorrhage, and pulmonary, cerebral and hepatic arteriovenous malformations; all secondary manifestations of the underlying vascular dysplasia. Ref.3 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily. Contains 1 GS domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Signal Transmembrane
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	angiogenesis Inferred from mutant phenotype. Source: HGNC negative regulation of cell growth Inferred from direct assay. Source: UniProtKB negative regulation of cell proliferation Inferred from mutant phenotype. Source: HGNC negative regulation of endothelial cell migration Inferred from direct assay. Source: UniProtKB negative regulation of focal adhesion assembly Inferred from mutant phenotype. Source: HGNC positive regulation of BMP signaling pathway Inferred from direct assay. Source: UniProtKB positive regulation of transcription Inferred from direct assay. Source: HGNC protein amino acid phosphorylation Inferred from direct assay. Source: HGNC regulation of blood pressure Ref.12 Inferred from mutant phenotype. Source: HGNC transforming growth factor beta receptor signaling pathway Inferred from direct assay. Source: HGNC wound healing, spreading of epidermal cells Inferred from mutant phenotype. Source: HGNC
Cellular component	cell surface Ref.2 Inferred from direct assay. Source: MGI cytoplasm Inferred from direct assay. Source: HPA integral to plasma membrane Ref.2 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from direct assay. Source: HGNC SMAD binding Inferred from direct assay. Source: HGNC activin binding Ref.2 Inferred from direct assay. Source: UniProtKB activin receptor activity, type I Ref.2 Inferred from direct assay. Source: MGI magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW transforming growth factor beta binding Ref.2 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 503	482	Serine/threonine-protein kinase receptor R3		PRO_0000024420
Regions
	Topological domain	22 – 118	97	Extracellular Potential
	Transmembrane	119 – 141	23	Potential
	Topological domain	142 – 503	362	Cytoplasmic Potential
	Domain	172 – 201	30	GS
	Domain	202 – 492	291	Protein kinase
	Nucleotide binding	208 – 216	9	ATP By similarity
Sites
	Active site	330	1	Proton acceptor By similarity
	Binding site	229	1	ATP By similarity
Amino acid modifications
	Modified residue	155	1	Phosphoserine By similarity
	Glycosylation	98	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	48 – 49	2	GA → EP in HHT2.		VAR_026784
	Natural variant	48	1	G → R in HHT2. Ref.14		VAR_026785
	Natural variant	50	1	W → C in HHT2; retained in the cell cytoplasm in the endoplasmic reticulum. Ref.3 Ref.9 Ref.12		VAR_006204
	Natural variant	51	1	C → Y in HHT2. Ref.8		VAR_006205
	Natural variant	67	1	R → Q in HHT2; retained in the cell cytoplasm in the endoplasmic reticulum. Ref.3 Ref.12		VAR_006206
	Natural variant	67	1	R → W in HHT2. Ref.15		VAR_026786
	Natural variant	77	1	C → W in HHT2; retained in the cell cytoplasm in the endoplasmic reticulum. Ref.8 Ref.12		VAR_006207
	Natural variant	96	1	N → D in HHT2. Ref.8		VAR_006208
	Natural variant	179	1	D → A in HHT2; mutant protein is capable of targeting the cell surface appropriately. Ref.12		VAR_026787
	Natural variant	211	1	G → D in HHT2; retained in the cell cytoplasm in the endoplasmic reticulum. dbSNP rs28936687. Ref.12		VAR_026788
	Natural variant	215	1	E → K in HHT2. Ref.14		VAR_026789
	Natural variant	223	1	G → R in HHT2. Ref.14		VAR_026790
	Natural variant	229	1	K → R in HHT2. Ref.14		VAR_026791
	Natural variant	232	1	Missing in HHT2; mutant protein is capable of targeting the cell surface appropriately.		VAR_006209
	Natural variant	233	1	Missing in HHT2.		VAR_026792
	Natural variant	245	1	I → N: dbSNP rs1804508.		VAR_011717
	Natural variant	254	1	Missing in HHT2; retained in the cell cytoplasm in the endoplasmic reticulum.		VAR_026793
	Natural variant	285	1	L → F in HHT2. Ref.14		VAR_026794
	Natural variant	306	1	A → P in HHT2. Ref.14		VAR_026795
	Natural variant	314	1	H → Y in HHT2. Ref.14		VAR_026796
	Natural variant	333	1	S → I in HHT2; retained in the cell cytoplasm in the endoplasmic reticulum. Ref.3 Ref.9 Ref.12		VAR_006210
	Natural variant	337	1	L → P in HHT2. Ref.14		VAR_026797
	Natural variant	344	1	C → Y in HHT2; retained in the cell cytoplasm in the endoplasmic reticulum. dbSNP rs28936688. Ref.9 Ref.12		VAR_026798
	Natural variant	347	1	A → P in HHT2. Ref.14		VAR_026799
	Natural variant	374	1	R → Q in HHT2; retained in the cell cytoplasm in the endoplasmic reticulum. Ref.12 Ref.14		VAR_026800
	Natural variant	374	1	R → W in HHT2. dbSNP rs28936401. Ref.3 Ref.10 Ref.12 Ref.15		VAR_006211
	Natural variant	376	1	M → R in HHT2. dbSNP rs28936399. Ref.7		VAR_006212
	Natural variant	376	1	M → V in HHT2. Ref.14		VAR_026801
	Natural variant	378	1	P → L in HHT2; retained in the cell cytoplasm in the endoplasmic reticulum. Ref.12		VAR_026802
	Natural variant	379	1	E → K in HHT2. Ref.14 Ref.15		VAR_026803
	Natural variant	397	1	D → G in HHT2. Ref.14		VAR_026804
	Natural variant	398	1	I → N in HHT2. dbSNP rs28936400. Ref.10		VAR_026805
	Natural variant	399	1	W → S in HHT2. dbSNP rs28936402. Ref.12		VAR_026806
	Natural variant	407	1	E → D in HHT2. Ref.9 Ref.15		VAR_026807
	Natural variant	411	1	R → P in HHT2. Ref.14		VAR_026808
	Natural variant	411	1	R → Q in HHT2; retained in the cell cytoplasm in the endoplasmic reticulum. dbSNP rs28936398. Ref.7 Ref.12 Ref.14		VAR_006213
	Natural variant	411	1	R → W in HHT2. Ref.11 Ref.14 Ref.15		VAR_026809
	Natural variant	424	1	P → T in HHT2. Ref.3		VAR_006214
	Natural variant	425	1	F → L in HHT2. Ref.14		VAR_026810
	Natural variant	425	1	F → V in HHT2. Ref.15		VAR_026811
	Natural variant	425	1	Missing in HHT2.		VAR_026812
	Natural variant	479	1	R → L in HHT2. Ref.14		VAR_026813
	Natural variant	482	1	A → V in HHT2. Ref.14		VAR_026814
	Natural variant	484	1	R → W in HHT2. Ref.11 Ref.14		VAR_026815
	Natural variant	487	1	K → T in HHT2; mutant protein is capable of targeting the cell surface appropriately. Ref.12		VAR_026816
Experimental info
	Sequence conflict	172	1	S → T in CAA80255. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P37023-1 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: 074522AA802325DD	FASTA	503	56,124
	10 20 30 40 50 60 MTLGSPRKGL LMLLMALVTQ GDPVKPSRGP LVTCTCESPH CKGPTCRGAW CTVVLVREEG 70 80 90 100 110 120 RHPQEHRGCG NLHRELCRGR PTEFVNHYCC DSHLCNHNVS LVLEATQPPS EQPGTDGQLA 130 140 150 160 170 180 LILGPVLALL ALVALGVLGL WHVRRRQEKQ RGLHSELGES SLILKASEQG DSMLGDLLDS 190 200 210 220 230 240 DCTTGSGSGL PFLVQRTVAR QVALVECVGK GRYGEVWRGL WHGESVAVKI FSSRDEQSWF 250 260 270 280 290 300 RETEIYNTVL LRHDNILGFI ASDMTSRNSS TQLWLITHYH EHGSLYDFLQ RQTLEPHLAL 310 320 330 340 350 360 RLAVSAACGL AHLHVEIFGT QGKPAIAHRD FKSRNVLVKS NLQCCIADLG LAVMHSQGSD 370 380 390 400 410 420 YLDIGNNPRV GTKRYMAPEV LDEQIRTDCF ESYKWTDIWA FGLVLWEIAR RTIVNGIVED 430 440 450 460 470 480 YRPPFYDVVP NDPSFEDMKK VVCVDQQTPT IPNRLAADPV LSGLAQMMRE CWYPNPSARL 490 500 TALRIKKTLQ KISNSPEKPK VIQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity." ten Dijke P., Ichijo H., Franzen P., Schulz P., Saras J., Toyoshima H., Heldin C.-H., Miyazono K. Oncogene 8:2879-2887(1993) [PubMed: 8397373] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"Identification of human activin and TGF beta type I receptors that form heteromeric kinase complexes with type II receptors." Attisano L., Carcamo J., Ventura F., Weis F.M., Massague J., Wrana J.L. Cell 75:671-680(1993) [PubMed: 8242742] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The activin receptor-like kinase 1 gene: genomic structure and mutations in hereditary hemorrhagic telangiectasia type 2." 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. Am. J. Hum. Genet. 61:60-67(1997) [PubMed: 9245985] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HHT2 CYS-50; GLN-67; ILE-333; TRP-374 AND THR-424.
[4]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	"Mutations in the activin receptor-like kinase 1 gene in hereditary haemorrhagic telangiectasia type 2." 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. Nat. Genet. 13:189-194(1996) [PubMed: 8640225] [Abstract] Cited for: VARIANTS HHT2 SER-232 DEL; ARG-376 AND GLN-411.
[8]	"Novel missense and frameshift mutations in the activin receptor-like kinase-1 gene in hereditary hemorrhagic telangiectasia." Klaus D.J., Gallione C.J., Anthony K., Yeh E.Y., Yu J., Lux A., Johnson D.W., Marchuk D.A. Hum. Mutat. 12:137-137(1998) [PubMed: 10694922] [Abstract] Cited for: VARIANTS HHT2 TYR-51; TRP-77 AND ASP-96.
[9]	"Analysis of ALK-1 and endoglin in newborns from families with hereditary hemorrhagic telangiectasia type 2." Abdalla S.A., Pece-Barbara N., Vera S., Tapia E., Paez E., Bernabeu C., Letarte M. Hum. Mol. Genet. 9:1227-1237(2000) [PubMed: 10767348] [Abstract] Cited for: VARIANTS HHT2 GLY-48-49-ALA DELINS EP; CYS-50; SER-232 DEL; ILE-333; TYR-344 AND ASP-407.
[10]	"Mutations in the ALK-1 gene and the phenotype of hereditary hemorrhagic telangiectasia in two large Danish families." Kjeldsen A.D., Brusgaard K., Poulsen L., Kruse T., Rasmussen K., Green A., Vase P. Am. J. Med. Genet. 98:298-302(2001) [PubMed: 11170071] [Abstract] Cited for: VARIANTS HHT2 TRP-374 AND ASN-398.
[11]	"Clinical and molecular genetic features of pulmonary hypertension in patients with hereditary hemorrhagic telangiectasia." 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. N. Engl. J. Med. 345:325-334(2001) [PubMed: 11484689] [Abstract] Cited for: VARIANTS HHT2 ASP-254 DEL; TRP-411 AND TRP-484.
[12]	"Molecular and functional analysis identifies ALK-1 as the predominant cause of pulmonary hypertension related to hereditary haemorrhagic telangiectasia." 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. 40:865-871(2003) [PubMed: 14684682] [Abstract] Cited for: VARIANTS HHT2 ALA-179; ASP-211; TYR-344; TRP-374; GLN-374; SER-399; GLN-411 AND THR-487, 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.
[13]	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)
[14]	"Molecular screening of ALK1/ACVRL1 and ENG genes in hereditary hemorrhagic telangiectasia in France." 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. Hum. Mutat. 23:289-299(2004) [PubMed: 15024723] [Abstract] Cited for: 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.
[15]	"Hepatic manifestation is associated with ALK1 in hereditary hemorrhagic telangiectasia: identification of five novel ALK1 and one novel ENG mutations." Kuehl H.K.A., Caselitz M., Hasenkamp S., Wagner S., El-Harith E.-H.A., Manns M.P., Stuhrmann M. Hum. Mutat. 25:320-320(2005) [PubMed: 15712270] [Abstract] Cited for: VARIANTS HHT2 TRP-67; TRP-374; LYS-379; ASP-407; TRP-411; VAL-425 AND PHE-425 DEL.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z22533 mRNA. Translation: CAA80255.1. L17075 mRNA. Translation: AAA16160.1. U77713 , U77707, U77708, U77709, U77710, U77711, U77712 Genomic DNA. Translation: AAB61900.1. AC025259 Genomic DNA. No translation available. CH471111 Genomic DNA. Translation: EAW58213.1. BC042637 mRNA. Translation: AAH42637.1.
IPI	IPI00293271.
PIR	A49431.
RefSeq	NP_000011.2. NP_001070869.1.
UniGene	Hs.591026
3D structure databases
SMR	P37023. Positions 172-493.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-423N. DIP-5938N.
STRING	P37023.
PTM databases
PhosphoSite	P37023.
Proteomic databases
PRIDE	P37023.
Genome annotation databases
Ensembl	ENST00000267008; ENSP00000267008; ENSG00000139567; Homo sapiens. [Genome view] ENST00000388922; ENSP00000373574; ENSG00000139567; Homo sapiens. [Genome view]
GeneID	94.
KEGG	hsa:94.
UCSC	uc001rzj.1. human.
Organism-specific databases
CTD	94.
GeneCards	GC12P050587.
HGNC	HGNC:175. ACVRL1.
HPA	HPA007041.
MIM	600376. phenotype. 601284. gene.
Orphanet	422. Idiopathic and/or familial pulmonary arterial hypertension. 774. Rendu-Osler-Weber disease.
PharmGKB	PA24496.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG17435.
HOGENOM	HBG314718.
HOVERGEN	P37023.
InParanoid	P37023.
OMA	RQEKQRG.
OrthoDB	EOG983GQ0.
Enzyme and pathway databases
BRENDA	2.7.10.2. 247. 2.7.11.30. 247.
Gene expression databases
ArrayExpress	P37023.
Bgee	P37023.
CleanEx	HS_ACVRL1.
Genevestigator	P37023.
GermOnline	ENSG00000139567. Homo sapiens.
Family and domain databases
InterPro	IPR000333. Activin_II_recpt. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR003605. TGF_beta_rcpt_GS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. PF08515. TGF_beta_GS. 1 hit. [Graphical view]
PRINTS	PR00653. ACTIVIN2R.
SMART	SM00467. GS. 1 hit. [Graphical view]
PROSITE	PS51256. GS. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00171. Adenosine triphosphate.
NextBio	355.
SOURCE	Search...

Entry information

Entry name

ACVL1_HUMAN

Accession

Primary (citable) accession number: P37023
Secondary accession number(s): A6NGA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	December 15, 1998
Last modified:	January 19, 2010
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.