| Tag | Content |
|---|
| EKPD ID | EKS-HOS-00282 |
| Classification | | Group/Family | Score | E-Value | Start | End | Domain Length |
|---|
| TKL/STKR | 456.9 | 1.4E-136 | 155 | 442 | 288 |
|
| Status | Reviewed |
| Ensembl Protein | ENSP00000442885 |
| UniProt Accession | P36896; B7Z5L8; B7Z5W5; Q15479; Q15480; Q15481; Q15482; |
| Protein Name | Activin receptor type-1B |
| Protein Synonyms/Alias | Activin receptor type IB; ACTR-IB; Activin receptor-like kinase 4; ALK-4; Serine/threonine-protein kinase receptor R2; SKR2; |
| Gene Name | ACVR1B |
| Gene Synonyms/Alias | ACVR1B; ACVRLK4, ALK4; |
| Ensembl Information | |
| Organism | Homo sapiens |
| Functional Description | Transmembrane serine/threonine kinase activin type-1receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a 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, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas 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 such as ACVR1B. 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. ACVR1B also phosphorylates TDP2. |
| Protein Length | 453 |
Protein Sequence
(FASTA) | | MVSIFNLDGM EHHVRTCIPK VELVPAGKPF YCLSSEDLRN THCCYTDYCN RIDLRVPSGH 60 | | LKEPEHPSMW GPVELVGIIA GPVFLLFLII IIVFLVINYH QRVYHNRQRL DMEDPSCEMC 120 | | LSKDKTLQDL VYDLSTSGSG SGLPLFVQRT VARTIVLQEI IGKGRFGEVW RGRWRGGDVA 180 | | VKIFSSREER SWFREAEIYQ TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD 240 | | YLNRYTVTIE GMIKLALSAA SGLAHLHMEI VGTQGKPGIA HRDLKSKNIL VKKNGMCAIA 300 | | DLGLAVRHDA VTDTIDIAPN QRVGTKRYMA PEVLDETINM KHFDSFKCAD IYALGLVYWE 360 | | IARRCNSGGV HEEYQLPYYD LVPSDPSIEE MRKVVCDQKL RPNIPNWWQS YEALRVMGKM 420 | | MRECWYANGA ARLTALRIKK TLSQLSVQED VKI 453 |
|
Nucleotide Sequence
(FASTA) | | ATGGTTTCCA TTTTCAATCT GGATGGGATG GAGCACCATG TGCGCACCTG CATCCCCAAA 60 | | GTGGAGCTGG TCCCTGCCGG GAAGCCCTTC TACTGCCTGA GCTCGGAGGA CCTGCGCAAC 120 | | ACCCACTGCT GCTACACTGA CTACTGCAAC AGGATCGACT TGAGGGTGCC CAGTGGTCAC 180 | | CTCAAGGAGC CTGAGCACCC GTCCATGTGG GGCCCGGTGG AGCTGGTAGG CATCATCGCC 240 | | GGCCCGGTGT TCCTCCTGTT CCTCATCATC ATCATTGTTT TCCTTGTCAT TAACTATCAT 300 | | CAGCGTGTCT ATCACAACCG CCAGAGACTG GACATGGAAG ATCCCTCATG TGAGATGTGT 360 | | CTCTCCAAAG ACAAGACGCT CCAGGATCTT GTCTACGATC TCTCCACCTC AGGGTCTGGC 420 | | TCAGGGTTAC CCCTCTTTGT CCAGCGCACA GTGGCCCGAA CCATCGTTTT ACAAGAGATT 480 | | ATTGGCAAGG GTCGGTTTGG GGAAGTATGG CGGGGCCGCT GGAGGGGTGG TGATGTGGCT 540 | | GTGAAAATAT TCTCTTCTCG TGAAGAACGG TCTTGGTTCA GGGAAGCAGA GATATACCAG 600 | | ACGGTCATGC TGCGCCATGA AAACATCCTT GGATTTATTG CTGCTGACAA TAAAGATAAT 660 | | GGCACCTGGA CACAGCTGTG GCTTGTTTCT GACTATCATG AGCACGGGTC CCTGTTTGAT 720 | | TATCTGAACC GGTACACAGT GACAATTGAG GGGATGATTA AGCTGGCCTT GTCTGCTGCT 780 | | AGTGGGCTGG CACACCTGCA CATGGAGATC GTGGGCACCC AAGGGAAGCC TGGAATTGCT 840 | | CATCGAGACT TAAAGTCAAA GAACATTCTG GTGAAGAAAA ATGGCATGTG TGCCATAGCA 900 | | GACCTGGGCC TGGCTGTCCG TCATGATGCA GTCACTGACA CCATTGACAT TGCCCCGAAT 960 | | CAGAGGGTGG GGACCAAACG ATACATGGCC CCTGAAGTAC TTGATGAAAC CATTAATATG 1020 | | AAACACTTTG ACTCCTTTAA ATGTGCTGAT ATTTATGCCC TCGGGCTTGT ATATTGGGAG 1080 | | ATTGCTCGAA GATGCAATTC TGGAGGAGTC CATGAAGAAT ATCAGCTGCC ATATTACGAC 1140 | | TTAGTGCCCT CTGACCCTTC CATTGAGGAA ATGCGAAAGG TTGTATGTGA TCAGAAGCTG 1200 | | CGTCCCAACA TCCCCAACTG GTGGCAGAGT TATGAGGCAC TGCGGGTGAT GGGGAAGATG 1260 | | ATGCGAGAGT GTTGGTATGC CAACGGCGCA GCCCGCCTGA CGGCCCTGCG CATCAAGAAG 1320 | | ACCCTCTCCC AGCTCAGCGT GCAGGAAGAC GTGAAGATCT AA 1362 |
|
| Domain Profile | S: 1 lklleligkGrygeVwkaklrgeevAvKifstedeaswkrEkeiyqtvllrhenilqfia 60 | + l+e+igkGr+geVw++++rg +vAvKifs+++e+sw+rE+eiyqtv+lrhenil+fia | Q: 155 IVLQEIIGKGRFGEVWRGRWRGGDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIA 214 | 5789******************************************************** |
| S: 61 adkkeedsltelllvteyhekgsLsdyLkretldveellrlalslasGlahLHeeivgtk 120 | ad+k+++++t+l+lv++yhe+gsL+dyL+r+t+++e +++lals+asGlahLH+eivgt+ | Q: 215 ADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTIEGMIKLALSAASGLAHLHMEIVGTQ 274 | ************************************************************ |
| S: 121 gkkKpaiaHRDlkskNilvkkdltcciaDlGLalkleeekeeldlaansqvGtkRYmaPE 180 | g Kp iaHRDlkskNilvkk+++c+iaDlGLa+++++ ++++d+a n++vGtkRYmaPE | Q: 275 G--KPGIAHRDLKSKNILVKKNGMCAIADLGLAVRHDAVTDTIDIAPNQRVGTKRYMAPE 332 | *..********************************************************* |
| S: 181 vleealnlkdfeafkraDvYslgLvlWEvasRceevdeeveeyklpfeevvgsdPsleem 240 | vl+e++n+k+f++fk+aD+Y+lgLv+WE+a+Rc++ ++++eey+lp+++ v+sdPs+eem | Q: 333 VLDETINMKHFDSFKCADIYALGLVYWEIARRCNS-GGVHEEYQLPYYDLVPSDPSIEEM 391 | ***********************************.************************ |
| S: 241 kevvvekklrPkipeawkkkealkelsklleecWdadpeaRltalrvkkrl 291 | ++vv+++klrP+ip+ w++ eal+++ k+++ecW+a+++aRltalr+kk+l | Q: 392 RKVVCDQKLRPNIPNWWQSYEALRVMGKMMRECWYANGAARLTALRIKKTL 442 | *************************************************97 |
|
Domain Sequence
(FASTA) | | IVLQEIIGKG RFGEVWRGRW RGGDVAVKIF SSREERSWFR EAEIYQTVML RHENILGFIA 60 | | ADNKDNGTWT QLWLVSDYHE HGSLFDYLNR YTVTIEGMIK LALSAASGLA HLHMEIVGTQ 120 | | GKPGIAHRDL KSKNILVKKN GMCAIADLGL AVRHDAVTDT IDIAPNQRVG TKRYMAPEVL 180 | | DETINMKHFD SFKCADIYAL GLVYWEIARR CNSGGVHEEY QLPYYDLVPS DPSIEEMRKV 240 | | VCDQKLRPNI PNWWQSYEAL RVMGKMMREC WYANGAARLT ALRIKKTL 288 |
|
| Keyword | Alternative splicing; ATP-binding; Cell membrane; Complete proteome; Glycoprotein; Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Serine/threonine-protein kinase; Signal; Transferase; Transmembrane; Transmembrane helix; Ubl conjugation. |
| Sequence Source | Ensembl |
| Orthology | |
| Gene Ontology | | GO:0048179 | ; C:activin receptor complex | | GO:0009986 | ; C:cell surface | | GO:0005887 | ; C:integral to plasma membrane | | GO:0016361 | ; F:activin receptor activity, type I | | GO:0005524 | ; F:ATP binding | | GO:0046872 | ; F:metal ion binding | | GO:0004702 | ; F:receptor signaling protein serine/threonine kinase activity | | GO:0046332 | ; F:SMAD binding | | GO:0005024 | ; F:transforming growth factor beta-activated receptor activity | | GO:0007417 | ; P:central nervous system development | | GO:0046545 | ; P:development of primary female sexual characteristics | | GO:0000082 | ; P:G1/S transition of mitotic cell cycle | | GO:0001942 | ; P:hair follicle development | | GO:0001701 | ; P:in utero embryonic development | | GO:0006917 | ; P:induction of apoptosis | | GO:0030308 | ; P:negative regulation of cell growth | | GO:0038092 | ; P:nodal signaling pathway | | GO:0018107 | ; P:peptidyl-threonine phosphorylation | | GO:0032927 | ; P:positive regulation of activin receptor signaling pathway | | GO:0045648 | ; P:positive regulation of erythrocyte differentiation | | GO:0010862 | ; P:positive regulation of pathway-restricted SMAD protein phosphorylation | | GO:0045944 | ; P:positive regulation of transcription from RNA polymerase II promoter | | GO:1901165 | ; P:positive regulation of trophoblast cell migration | | GO:0046777 | ; P:protein autophosphorylation | | GO:0006355 | ; P:regulation of transcription, DNA-dependent | | GO:0023014 | ; P:signal transduction by phosphorylation |
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| InterPros | |
| Pfam | |
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| Prints | |
| Created Date | 20-Feb-2013 |