EKS-HOS-00289

Eukaryotic Protein Kinase & Protein Phosphatase Database

Tag

Content

EKPD ID

EKS-HOS-00289

Classification

Group/Family	Score	E-Value	Start	End	Domain Length
TKL/STKR	408.5	7.4E-122	190	477	288

Status

Reviewed

Ensembl Protein

ENSP00000340361

UniProt Accession

Q13705; Q4VAV0;

Protein Name

Activin receptor type-2B

Protein Synonyms/Alias

Activin receptor type IIB; ACTR-IIB;

Gene Name

ACVR2B

Gene Synonyms/Alias

ACVR2B;

Ensembl Information

Ensembl Gene ID	Ensembl Protein ID	Ensembl Transcript ID
ENSG00000114739	ENSP00000340361	ENST00000352511

Organism

Homo sapiens

Functional Description

Transmembrane serine/threonine kinase activin type-2receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor.

Protein Length

512

Protein Sequence
(FASTA)

MTAPWVALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GEQDKRLHCY 60

ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEAG 120

GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP 180

PSPLVGLKPL QLLEIKARGR FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK 240

HENLLQFIAA EKRGSNLEVE LWLITAFHDK GSLTDYLKGN IITWNELCHV AETMSRGLSY 300

LHEDVPWCRG EGHKPSIAHR DFKSKNVLLK SDLTAVLADF GLAVRFEPGK PPGDTHGQVG 360

TRRYMAPEVL EGAINFQRDA FLRIDMYAMG LVLWELVSRC KAADGPVDEY MLPFEEEIGQ 420

HPSLEELQEV VVHKKMRPTI KDHWLKHPGL AQLCVTIEEC WDHDAEARLS AGCVEERVSL 480

IRRSVNGTTS DCLVSLVTSV TNVDLPPKES SI 512

Nucleotide Sequence
(FASTA)

ATGACGGCGC CCTGGGTGGC CCTCGCCCTC CTCTGGGGAT CGCTGTGCGC CGGCTCTGGG 60

CGTGGGGAGG CTGAGACACG GGAGTGCATC TACTACAACG CCAACTGGGA GCTGGAGCGC 120

ACCAACCAGA GCGGCCTGGA GCGCTGCGAA GGCGAGCAGG ACAAGCGGCT GCACTGCTAC 180

GCCTCCTGGC GCAACAGCTC TGGCACCATC GAGCTCGTGA AGAAGGGCTG CTGGCTAGAT 240

GACTTCAACT GCTACGATAG GCAGGAGTGT GTGGCCACTG AGGAGAACCC CCAGGTGTAC 300

TTCTGCTGCT GTGAAGGCAA CTTCTGCAAC GAACGCTTCA CTCATTTGCC AGAGGCTGGG 360

GGCCCGGAAG TCACGTACGA GCCACCCCCG ACAGCCCCCA CCCTGCTCAC GGTGCTGGCC 420

TACTCACTGC TGCCCATCGG GGGCCTTTCC CTCATCGTCC TGCTGGCCTT TTGGATGTAC 480

CGGCATCGCA AGCCCCCCTA CGGTCATGTG GACATCCATG AGGACCCTGG GCCTCCACCA 540

CCATCCCCTC TGGTGGGCCT GAAGCCACTG CAGCTGCTGG AGATCAAGGC TCGGGGGCGC 600

TTTGGCTGTG TCTGGAAGGC CCAGCTCATG AATGACTTTG TAGCTGTCAA GATCTTCCCA 660

CTCCAGGACA AGCAGTCGTG GCAGAGTGAA CGGGAGATCT TCAGCACACC TGGCATGAAG 720

CACGAGAACC TGCTACAGTT CATTGCTGCC GAGAAGCGAG GCTCCAACCT CGAAGTAGAG 780

CTGTGGCTCA TCACGGCCTT CCATGACAAG GGCTCCCTCA CGGATTACCT CAAGGGGAAC 840

ATCATCACAT GGAACGAACT GTGTCATGTA GCAGAGACGA TGTCACGAGG CCTCTCATAC 900

CTGCATGAGG ATGTGCCCTG GTGCCGTGGC GAGGGCCACA AGCCGTCTAT TGCCCACAGG 960

GACTTTAAAA GTAAGAATGT ATTGCTGAAG AGCGACCTCA CAGCCGTGCT GGCTGACTTT 1020

GGCTTGGCTG TTCGATTTGA GCCAGGGAAA CCTCCAGGGG ACACCCACGG ACAGGTAGGC 1080

ACGAGACGGT ACATGGCTCC TGAGGTGCTC GAGGGAGCCA TCAACTTCCA GAGAGATGCC 1140

TTCCTGCGCA TTGACATGTA TGCCATGGGG TTGGTGCTGT GGGAGCTTGT GTCTCGCTGC 1200

AAGGCTGCAG ACGGACCCGT GGATGAGTAC ATGCTGCCCT TTGAGGAAGA GATTGGCCAG 1260

CACCCTTCGT TGGAGGAGCT GCAGGAGGTG GTGGTGCACA AGAAGATGAG GCCCACCATT 1320

AAAGATCACT GGTTGAAACA CCCGGGCCTG GCCCAGCTTT GTGTGACCAT CGAGGAGTGC 1380

TGGGACCATG ATGCAGAGGC TCGCTTGTCC GCGGGCTGTG TGGAGGAGCG GGTGTCCCTG 1440

ATTCGGAGGT CGGTCAACGG CACTACCTCG GACTGTCTCG TTTCCCTGGT GACCTCTGTC 1500

ACCAATGTGG ACCTGCCCCC TAAAGAGTCA AGCATCTAA 1539

Domain Profile

S: 1     lklleligkGrygeVwkaklrgeevAvKifstedeaswkrEkeiyqtvllrhenilqfia  60

         l+lle+ ++Gr+g+Vwka+l+++ vAvKif+ +d++sw++E+ei++t+ ++hen+lqfia

Q: 190   LQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMKHENLLQFIA  249

         6899********************************************************

S: 61    adkkeedsltelllvteyhekgsLsdyLkretldveellrlalslasGlahLHeeivgtk  120

         a+k+ +++++el+l+t++h+kgsL+dyLk ++++++el+++a+++++Gl++LHe++++++

Q: 250   AEKRGSNLEVELWLITAFHDKGSLTDYLKGNIITWNELCHVAETMSRGLSYLHEDVPWCR  309

         ************************************************************

S: 121   g.kkKpaiaHRDlkskNilvkkdltcciaDlGLalkleeekeeldlaansqvGtkRYmaP  179

         g  +Kp+iaHRD+kskN+l+k+dlt+++aD+GLa+++e  k   d  ++ qvGt+RYmaP

Q: 310   GeGHKPSIAHRDFKSKNVLLKSDLTAVLADFGLAVRFEPGKPPGD--THGQVGTRRYMAP  367

         *99***************************************888..79***********

S: 180   EvleealnlkdfeafkraDvYslgLvlWEvasRceevdeeveeyklpfeevvgsdPslee  239

         Evle+a+n+++ +af r+D+Y++gLvlWE++sRc+++d+ v+ey+lpfee++g++Pslee

Q: 368   EVLEGAINFQR-DAFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQHPSLEE  426

         **********9.9***********************************************

S: 240   mkevvvekklrPkipeawkkkealkelsklleecWdadpeaRltalrvkkr  290

         ++evvv+kk+rP+i+++w k++ l++l+ ++eecWd+d+eaRl+a +v++r

Q: 427   LQEVVVHKKMRPTIKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEER  477

         ************************************************998

Domain Sequence
(FASTA)

LQLLEIKARG RFGCVWKAQL MNDFVAVKIF PLQDKQSWQS EREIFSTPGM KHENLLQFIA 60

AEKRGSNLEV ELWLITAFHD KGSLTDYLKG NIITWNELCH VAETMSRGLS YLHEDVPWCR 120

GEGHKPSIAH RDFKSKNVLL KSDLTAVLAD FGLAVRFEPG KPPGDTHGQV GTRRYMAPEV 180

LEGAINFQRD AFLRIDMYAM GLVLWELVSR CKAADGPVDE YMLPFEEEIG QHPSLEELQE 240

VVVHKKMRPT IKDHWLKHPG LAQLCVTIEE CWDHDAEARL SAGCVEER 288

Keyword

3D-structure; Alternative splicing; ATP-binding; Cell membrane; Complete proteome; Disease mutation; Disulfide bond; Glycoprotein; Heterotaxy; Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Serine/threonine-protein kinase; Signal; Transferase; Transmembrane; Transmembrane helix.

Sequence Source

Ensembl

Orthology

Ortholog group

Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Caenorhabditis elegans"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Ciona intestinalis"; ?>Ciona savignyi"; ?>Danio rerio"; ?>Drosophila melanogaster"; ?>Equus caballus"; ?>Felis catus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Meleagris gallopavo"; ?>Microcebus murinus"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Ornithorhynchus anatinus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Petromyzon marinus"; ?>Pongo abelii"; ?>Pteropus vampyrus"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tetraodon nigroviridis"; ?>Tupaia belangeri"; ?>Tursiops truncatus"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>

Gene Ontology

GO:0009986	; C:cell surface
GO:0005737	; C:cytoplasm
GO:0005887	; C:integral to plasma membrane
GO:0017002	; F:activin-activated receptor activity
GO:0005524	; F:ATP binding
GO:0046872	; F:metal ion binding
GO:0004674	; F:protein serine/threonine kinase activity
GO:0004712	; F:protein serine/threonine/tyrosine kinase activity
GO:0004702	; F:receptor signaling protein serine/threonine kinase activity
GO:0005024	; F:transforming growth factor beta-activated receptor activity
GO:0032147	; P:activation of protein kinase activity
GO:0009952	; P:anterior/posterior pattern specification
GO:0060840	; P:artery development
GO:0001974	; P:blood vessel remodeling
GO:0030509	; P:BMP signaling pathway
GO:0007368	; P:determination of left/right symmetry
GO:0048617	; P:embryonic foregut morphogenesis
GO:0001702	; P:gastrulation with mouth forming second
GO:0007507	; P:heart development
GO:0030073	; P:insulin secretion
GO:0001822	; P:kidney development
GO:0030324	; P:lung development
GO:0001946	; P:lymphangiogenesis
GO:0060836	; P:lymphatic endothelial cell differentiation
GO:0007498	; P:mesoderm development
GO:0042475	; P:odontogenesis of dentin-containing tooth
GO:0035265	; P:organ growth
GO:0060021	; P:palate development
GO:0031016	; P:pancreas development
GO:0032927	; P:positive regulation of activin receptor signaling pathway
GO:0030501	; P:positive regulation of bone mineralization
GO:0045669	; P:positive regulation of osteoblast differentiation
GO:0009791	; P:post-embryonic development
GO:0009749	; P:response to glucose stimulus
GO:0061298	; P:retina vasculature development in camera-type eye
GO:0023014	; P:signal transduction by phosphorylation
GO:0048705	; P:skeletal system morphogenesis
GO:0060841	; P:venous blood vessel development

KEGG

hsa:93

;

InterPros

IPR000333	; Activin_II/TGFBeta-II_recpt.
IPR015768	; Activin_II_recpt.
IPR000472	; Activin_rcpt.
IPR011009	; Kinase-like_dom.
IPR000719	; Prot_kinase_cat_dom.
IPR008271	; Ser/Thr_kinase_AS.

Pfam

PF01064	; Activin_recp; 1.
PF00069	; Pkinase; 1.

SMARTs

Prosites

PS00107	; PROTEIN_KINASE_ATP; FALSE_NEG.
PS50011	; PROTEIN_KINASE_DOM; 1.
PS00108	; PROTEIN_KINASE_ST; 1.

Prints

PR00653

; ACTIVIN2R.

Created Date

20-Feb-2013