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P27037

- AVR2A_HUMAN

UniProt

P27037 - AVR2A_HUMAN

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Protein
Activin receptor type-2A
Gene
ACVR2A, ACVR2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.

Cofactori

Magnesium or manganese By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei219 – 2191ATP By similarity
Active sitei322 – 3221Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi198 – 2069ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. coreceptor activity Source: BHF-UCL
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding Source: UniProtKB
  5. protein serine/threonine kinase activity Source: Reactome
  6. receptor signaling protein serine/threonine kinase activity Source: InterPro
  7. transforming growth factor beta-activated receptor activity Source: InterPro
  8. transmembrane receptor protein serine/threonine kinase activity Source: ProtInc

GO - Biological processi

  1. BMP signaling pathway Source: BHF-UCL
  2. Sertoli cell proliferation Source: Ensembl
  3. activin receptor signaling pathway Source: GOC
  4. anterior/posterior pattern specification Source: Ensembl
  5. cellular response to BMP stimulus Source: BHF-UCL
  6. determination of left/right symmetry Source: Ensembl
  7. embryonic skeletal system development Source: Ensembl
  8. gastrulation with mouth forming second Source: Ensembl
  9. mesoderm development Source: Ensembl
  10. penile erection Source: Ensembl
  11. positive regulation of activin receptor signaling pathway Source: HGNC
  12. positive regulation of bone mineralization Source: BHF-UCL
  13. positive regulation of erythrocyte differentiation Source: HGNC
  14. positive regulation of osteoblast differentiation Source: BHF-UCL
  15. positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  16. positive regulation of protein phosphorylation Source: MGI
  17. regulation of BMP signaling pathway Source: Ensembl
  18. regulation of nitric-oxide synthase activity Source: Ensembl
  19. sperm ejaculation Source: Ensembl
  20. spermatogenesis Source: Ensembl
  21. transmembrane receptor protein serine/threonine kinase signaling pathway Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_111057. Signaling by NODAL.
REACT_111059. Regulation of signaling by NODAL.
REACT_12034. Signaling by BMP.
REACT_150238. Signaling by Activin.
SignaLinkiP27037.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ACVR2A
Synonyms:ACVR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:173. ACVR2A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 135116Extracellular Reviewed prediction
Add
BLAST
Transmembranei136 – 16126Helical; Reviewed prediction
Add
BLAST
Topological domaini162 – 513352Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. cytoplasm Source: HGNC
  3. inhibin-betaglycan-ActRII complex Source: BHF-UCL
  4. integral component of plasma membrane Source: ProtInc
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24494.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 Reviewed prediction
Add
BLAST
Chaini20 – 513494Activin receptor type-2A
PRO_0000024398Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 60 By similarity
Glycosylationi43 – 431N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi50 ↔ 78 By similarity
Glycosylationi66 – 661N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi85 ↔ 104 By similarity
Disulfide bondi91 ↔ 103 By similarity
Disulfide bondi105 ↔ 110 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP27037.
PaxDbiP27037.
PRIDEiP27037.

PTM databases

PhosphoSiteiP27037.

Expressioni

Gene expression databases

ArrayExpressiP27037.
BgeeiP27037.
CleanExiHS_ACVR2A.
GenevestigatoriP27037.

Organism-specific databases

HPAiHPA046997.

Interactioni

Subunit structurei

Interacts with AIP1. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3 By similarity.

Protein-protein interaction databases

BioGridi106607. 17 interactions.
DIPiDIP-520N.
IntActiP27037. 1 interaction.
MINTiMINT-122188.
STRINGi9606.ENSP00000241416.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi191 – 1999
Beta strandi205 – 2117
Beta strandi214 – 2218
Helixi223 – 2253
Helixi226 – 23611
Beta strandi249 – 2568
Beta strandi258 – 26811
Helixi275 – 2817
Helixi286 – 30318
Beta strandi307 – 3104
Beta strandi313 – 3153
Beta strandi317 – 3193
Beta strandi327 – 3304
Beta strandi336 – 3383
Beta strandi345 – 3473
Helixi363 – 3653
Helixi368 – 3714
Helixi379 – 39820
Beta strandi404 – 4063
Helixi416 – 4194
Helixi425 – 4328
Helixi443 – 4464
Helixi449 – 46113
Helixi466 – 4683
Helixi472 – 48514

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q4TX-ray1.96A/B191-488[»]
3SOCX-ray1.95A/B191-488[»]
4ASXX-ray2.05A/B191-488[»]
ProteinModelPortaliP27037.
SMRiP27037. Positions 26-119, 191-486.

Miscellaneous databases

EvolutionaryTraceiP27037.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini192 – 485294Protein kinase
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000231495.
HOVERGENiHBG054502.
InParanoidiP27037.
KOiK04670.
OMAiEDPGNWI.
OrthoDBiEOG7JHM5B.
PhylomeDBiP27037.
TreeFamiTF352876.

Family and domain databases

InterProiIPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PfamiPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR00653. ACTIVIN2R.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P27037-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MGAAAKLAFA VFLISCSSGA ILGRSETQEC LFFNANWEKD RTNQTGVEPC    50
YGDKDKRRHC FATWKNISGS IEIVKQGCWL DDINCYDRTD CVEKKDSPEV 100
YFCCCEGNMC NEKFSYFPEM EVTQPTSNPV TPKPPYYNIL LYSLVPLMLI 150
AGIVICAFWV YRHHKMAYPP VLVPTQDPGP PPPSPLLGLK PLQLLEVKAR 200
GRFGCVWKAQ LLNEYVAVKI FPIQDKQSWQ NEYEVYSLPG MKHENILQFI 250
GAEKRGTSVD VDLWLITAFH EKGSLSDFLK ANVVSWNELC HIAETMARGL 300
AYLHEDIPGL KDGHKPAISH RDIKSKNVLL KNNLTACIAD FGLALKFEAG 350
KSAGDTHGQV GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELASR 400
CTAADGPVDE YMLPFEEEIG QHPSLEDMQE VVVHKKKRPV LRDYWQKHAG 450
MAMLCETIEE CWDHDAEARL SAGCVGERIT QMQRLTNIIT TEDIVTVVTM 500
VTNVDFPPKE SSL 513
Length:513
Mass (Da):57,848
Last modified:August 1, 1992 - v1
Checksum:iA89822E880979618
GO
Isoform 2 (identifier: P27037-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.

Note: No experimental confirmation available.

Show »
Length:405
Mass (Da):45,713
Checksum:iF0D4F7B18BD200AB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti258 – 2581S → R.1 Publication
Corresponds to variant rs34917571 [ dbSNP | Ensembl ].
VAR_032809
Natural varianti306 – 3061D → N in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_032810
Natural varianti367 – 3671A → T Found in a clear cell renal carcinoma case; somatic mutation. 1 Publication
VAR_064692

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 108108Missing in isoform 2.
VSP_054689Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131L → V in BAA06548. 1 Publication
Sequence conflicti204 – 2063GCV → PSL in BAA06548. 1 Publication
Sequence conflicti348 – 3481E → V in BAA06548. 1 Publication
Sequence conflicti507 – 5071P → L in AAH67417. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X63128 mRNA. Translation: CAA44839.1.
M93415 mRNA. Translation: AAA35504.1.
X62381 mRNA. Translation: CAA44245.1.
D31770 mRNA. Translation: BAA06548.1.
AK301629 mRNA. Translation: BAG63114.1.
AK314124 mRNA. Translation: BAG36815.1.
AC009480 Genomic DNA. Translation: AAX93050.1.
CH471058 Genomic DNA. Translation: EAX11561.1.
CH471058 Genomic DNA. Translation: EAX11562.1.
BC067418 mRNA. Translation: AAH67418.1.
BC067417 mRNA. Translation: AAH67417.1.
BC069707 mRNA. Translation: AAH69707.1.
CCDSiCCDS33301.1. [P27037-1]
CCDS63030.1. [P27037-2]
PIRiJQ1486.
RefSeqiNP_001265508.1. NM_001278579.1. [P27037-1]
NP_001265509.1. NM_001278580.1. [P27037-2]
NP_001607.1. NM_001616.4. [P27037-1]
UniGeneiHs.470174.

Genome annotation databases

EnsembliENST00000241416; ENSP00000241416; ENSG00000121989.
ENST00000404590; ENSP00000384338; ENSG00000121989.
ENST00000535787; ENSP00000439988; ENSG00000121989.
GeneIDi92.
KEGGihsa:92.
UCSCiuc002twg.3. human. [P27037-1]

Polymorphism databases

DMDMi114722.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
CGP resequencing studies

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X63128 mRNA. Translation: CAA44839.1 .
M93415 mRNA. Translation: AAA35504.1 .
X62381 mRNA. Translation: CAA44245.1 .
D31770 mRNA. Translation: BAA06548.1 .
AK301629 mRNA. Translation: BAG63114.1 .
AK314124 mRNA. Translation: BAG36815.1 .
AC009480 Genomic DNA. Translation: AAX93050.1 .
CH471058 Genomic DNA. Translation: EAX11561.1 .
CH471058 Genomic DNA. Translation: EAX11562.1 .
BC067418 mRNA. Translation: AAH67418.1 .
BC067417 mRNA. Translation: AAH67417.1 .
BC069707 mRNA. Translation: AAH69707.1 .
CCDSi CCDS33301.1. [P27037-1 ]
CCDS63030.1. [P27037-2 ]
PIRi JQ1486.
RefSeqi NP_001265508.1. NM_001278579.1. [P27037-1 ]
NP_001265509.1. NM_001278580.1. [P27037-2 ]
NP_001607.1. NM_001616.4. [P27037-1 ]
UniGenei Hs.470174.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3Q4T X-ray 1.96 A/B 191-488 [» ]
3SOC X-ray 1.95 A/B 191-488 [» ]
4ASX X-ray 2.05 A/B 191-488 [» ]
ProteinModelPortali P27037.
SMRi P27037. Positions 26-119, 191-486.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106607. 17 interactions.
DIPi DIP-520N.
IntActi P27037. 1 interaction.
MINTi MINT-122188.
STRINGi 9606.ENSP00000241416.

Chemistry

BindingDBi P27037.
ChEMBLi CHEMBL5616.
GuidetoPHARMACOLOGYi 1791.

PTM databases

PhosphoSitei P27037.

Polymorphism databases

DMDMi 114722.

Proteomic databases

MaxQBi P27037.
PaxDbi P27037.
PRIDEi P27037.

Protocols and materials databases

DNASUi 92.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000241416 ; ENSP00000241416 ; ENSG00000121989 .
ENST00000404590 ; ENSP00000384338 ; ENSG00000121989 .
ENST00000535787 ; ENSP00000439988 ; ENSG00000121989 .
GeneIDi 92.
KEGGi hsa:92.
UCSCi uc002twg.3. human. [P27037-1 ]

Organism-specific databases

CTDi 92.
GeneCardsi GC02P148602.
HGNCi HGNC:173. ACVR2A.
HPAi HPA046997.
MIMi 102581. gene.
neXtProti NX_P27037.
PharmGKBi PA24494.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000231495.
HOVERGENi HBG054502.
InParanoidi P27037.
KOi K04670.
OMAi EDPGNWI.
OrthoDBi EOG7JHM5B.
PhylomeDBi P27037.
TreeFami TF352876.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_111057. Signaling by NODAL.
REACT_111059. Regulation of signaling by NODAL.
REACT_12034. Signaling by BMP.
REACT_150238. Signaling by Activin.
SignaLinki P27037.

Miscellaneous databases

EvolutionaryTracei P27037.
GeneWikii ACVR2A.
GenomeRNAii 92.
NextBioi 347.
PROi P27037.
SOURCEi Search...

Gene expression databases

ArrayExpressi P27037.
Bgeei P27037.
CleanExi HS_ACVR2A.
Genevestigatori P27037.

Family and domain databases

InterProi IPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR000333. TGFB_receptor.
[Graphical view ]
PANTHERi PTHR23255. PTHR23255. 1 hit.
Pfami PF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR00653. ACTIVIN2R.
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  3. Geiser A.G.
    Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Mammary gland.
  4. Iimura T., Oida S.
    Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Colon and Hippocampus.
  6. "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.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  9. "Crystal structure of activin receptor type-IIa (ACVR2A) kinase domain in complex with dorsomorphin."
    Structural genomics consortium (SGC)
    Submitted (FEB-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 191-488 IN COMPLEX WITH DORSOMORPHIN.
  10. "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.
    , 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.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARG-258 AND ASN-306.
  11. Cited for: VARIANT THR-367.

Entry informationi

Entry nameiAVR2A_HUMAN
AccessioniPrimary (citable) accession number: P27037
Secondary accession number(s): B2RAB8
, B4DWQ2, D3DP85, Q53TH4, Q6NWV2, Q92474
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: September 3, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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