Activin receptor type-2A precursor - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Activin receptor type-2A
    EC=2.7.11.30
Alternative name(s):
    Activin receptor type IIA
      Short name=ACTR-IIA
      Short name=ACTRIIA

Gene names

Name:	ACVR2A
Synonyms:	ACVR2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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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 activin A, activin B and inhibin A.
Catalytic activity	ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
Cofactor	Magnesium or manganese By similarity.
Subunit structure	Interacts with AIP1. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3 By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein.
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily. Contains 1 protein kinase domain.

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Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	BMP signaling pathway Inferred from direct assay. Source: UniProtKB positive regulation of activin receptor signaling pathway Inferred from direct assay. Source: HGNC positive regulation of bone mineralization Inferred from mutant phenotype. Source: UniProtKB positive regulation of erythrocyte differentiation Inferred from direct assay. Source: HGNC positive regulation of osteoblast differentiation Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: HGNC integral to plasma membrane Ref.2 Traceable author statement. Source: ProtInc
Molecular function	inhibin beta-A binding Inferred from direct assay. Source: HGNC transmembrane receptor protein serine/threonine kinase activity Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Signal peptide

1 – 19

19

Potential

Chain

20 – 513

494

Activin receptor type-2A

Regions

Topological domain

20 – 135

116

Extracellular Potential

Transmembrane

136 – 161

26

Potential

Topological domain

162 – 513

352

Cytoplasmic Potential

Domain

192 – 485

294

Protein kinase

Nucleotide binding

198 – 206

9

ATP By similarity

Sites

Active site

322

1

Proton acceptor By similarity

Binding site

219

1

ATP By similarity

Amino acid modifications

Glycosylation

43

1

N-linked (GlcNAc...) Potential

Glycosylation

66

1

N-linked (GlcNAc...) Potential

Disulfide bond

30 ↔ 60

By similarity

Disulfide bond

50 ↔ 78

By similarity

Disulfide bond

85 ↔ 104

By similarity

Disulfide bond

91 ↔ 103

By similarity

Disulfide bond

105 ↔ 110

By similarity

Natural variations

Natural variant

258

1

S → R

Natural variant

306

1

D → N in a gastric adenocarcinoma sample; somatic mutation.

Experimental info

Sequence conflict

13

1

L → V in BAA06548. Ref.4

Sequence conflict

204 – 206

3

GCV → PSL in BAA06548. Ref.4

Sequence conflict

348

1

E → V in BAA06548. Ref.4

Sequence conflict

507

1

P → L in AAH67417. Ref.6

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Sequences

Sequence

Length

Mass (Da)

Tools

P27037-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: A89822E880979618
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FASTA

513

57,848

        10         20         30         40         50         60 
MGAAAKLAFA VFLISCSSGA ILGRSETQEC LFFNANWEKD RTNQTGVEPC YGDKDKRRHC 

        70         80         90        100        110        120 
FATWKNISGS IEIVKQGCWL DDINCYDRTD CVEKKDSPEV YFCCCEGNMC NEKFSYFPEM 

       130        140        150        160        170        180 
EVTQPTSNPV TPKPPYYNIL LYSLVPLMLI AGIVICAFWV YRHHKMAYPP VLVPTQDPGP 

       190        200        210        220        230        240 
PPPSPLLGLK PLQLLEVKAR GRFGCVWKAQ LLNEYVAVKI FPIQDKQSWQ NEYEVYSLPG 

       250        260        270        280        290        300 
MKHENILQFI GAEKRGTSVD VDLWLITAFH EKGSLSDFLK ANVVSWNELC HIAETMARGL 

       310        320        330        340        350        360 
AYLHEDIPGL KDGHKPAISH RDIKSKNVLL KNNLTACIAD FGLALKFEAG KSAGDTHGQV 

       370        380        390        400        410        420 
GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELASR CTAADGPVDE YMLPFEEEIG 

       430        440        450        460        470        480 
QHPSLEDMQE VVVHKKKRPV LRDYWQKHAG MAMLCETIEE CWDHDAEARL SAGCVGERIT 

       490        500        510 
QMQRLTNIIT TEDIVTVVTM VTNVDFPPKE SSL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the human activin receptor cDNA reveals high evolutionary conservation." Matzuk M.M., Bradley A. Biochim. Biophys. Acta 1130:105-108(1992) [PubMed: 1311955] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[2]	"Molecular cloning and binding properties of the human type II activin receptor." Donaldson C.J., Mathews L.S., Vale W.W. Biochem. Biophys. Res. Commun. 184:310-316(1992) [PubMed: 1314589] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[3]	Geiser A.G. Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary gland.
[4]	Iimura T., Oida S. Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] 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].
[7]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS ARG-258 AND ASN-306.
+	Additional computationally mapped references.

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Web resources

CGP resequencing studies

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Cross-references

Sequence databases
	X63128 mRNA. Translation: CAA44839.1. M93415 mRNA. Translation: AAA35504.1. X62381 mRNA. Translation: CAA44245.1. D31770 mRNA. Translation: BAA06548.1. BC067418 mRNA. Translation: AAH67418.1. AC009480 Genomic DNA. Translation: AAX93050.1. BC067417 mRNA. Translation: AAH67417.1. BC069707 mRNA. Translation: AAH69707.1.
PIR	JQ1486.
RefSeq	NP_001607.1.
UniGene	Hs.470174
3D structure databases
HSSP	HSSP built from PDB template 1BTE based on UniProtKB P27038.
SMR	P27037. Positions 26-119.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:520N.
IntAct	P27037.
PTM databases
PhosphoSite	P27037.
Genome annotation databases
Ensembl	ENSG00000121989. Homo sapiens. [Contig view]
GeneID	92.
KEGG	hsa:92.
NMPDR	fig\|9606.3.peg.18734.
Organism-specific databases
H-InvDB	HIX0029973.
HGNC	HGNC:173. ACVR2A.
MIM	102581. gene.
PharmGKB	PA24494.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P27037.
HOVERGEN	P27037.
Gene expression databases
ArrayExpress	P27037.
CleanEx	HS_ACVR2A.
GermOnline	ENSG00000121989. Homo sapiens.
Family and domain databases
InterPro	IPR000333. Activin_II_recpt. IPR015768. Activin_II_recpt_C. IPR000472. Activin_rcpt. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_bd_CS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. [Graphical view]
PANTHER	PTHR23255:SF10. Activin_II_recpt_C. 1 hit.
Pfam	PF01064. Activin_recp. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR00653. ACTIVIN2R.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
BLOCKS	Search...
Other Resources
LinkHub	P27037.
SOURCE	Search...
ProtoNet	Search...

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Entry information

Entry name

AVR2A_HUMAN

Accession

Primary (citable) accession number: P27037
Secondary accession number(s): Q53TH4, Q6NWV2, Q92474

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	July 22, 2008
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents