CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006679
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
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
 ACVRLK4; ALK4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
215VLQEIIGKGRFGEVWubiquitination[1, 2]
345SKNILVKKNGMCAIAubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
 Transmembrane serine/threonine kinase activin type-1 receptor 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. 
Sequence Annotation
 DOMAIN 177 206 GS.
 DOMAIN 207 497 Protein kinase.
 NP_BIND 213 221 ATP (By similarity).
 ACT_SITE 335 335 Proton acceptor (By similarity).
 BINDING 234 234 ATP (By similarity).
 MOD_RES 380 380 Phosphotyrosine.
 CARBOHYD 43 43 N-linked (GlcNAc...) (Potential).  
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
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 505 AA 
Protein Sequence
MAESAGASSF FPLVVLLLAG SGGSGPRGVQ ALLCACTSCL QANYTCETDG ACMVSIFNLD 60
GMEHHVRTCI PKVELVPAGK PFYCLSSEDL RNTHCCYTDY CNRIDLRVPS GHLKEPEHPS 120
MWGPVELVGI IAGPVFLLFL IIIIVFLVIN YHQRVYHNRQ RLDMEDPSCE MCLSKDKTLQ 180
DLVYDLSTSG SGSGLPLFVQ RTVARTIVLQ EIIGKGRFGE VWRGRWRGGD VAVKIFSSRE 240
ERSWFREAEI YQTVMLRHEN ILGFIAADNK DNGTWTQLWL VSDYHEHGSL FDYLNRYTVT 300
IEGMIKLALS AASGLAHLHM EIVGTQGKPG IAHRDLKSKN ILVKKNGMCA IADLGLAVRH 360
DAVTDTIDIA PNQRVGTKRY MAPEVLDETI NMKHFDSFKC ADIYALGLVY WEIARRCNSG 420
GVHEEYQLPY YDLVPSDPSI EEMRKVVCDQ KLRPNIPNWW QSYEALRVMG KMMRECWYAN 480
GAARLTALRI KKTLSQLSVQ EDVKI 505 
Gene Ontology
 GO:0009986; C:cell surface; IDA:HGNC.
 GO:0005887; C:integral to plasma membrane; IDA:HGNC.
 GO:0016361; F:activin receptor activity, type I; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:HGNC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004702; F:receptor signaling protein serine/threonine kinase activity; IEA:Compara.
 GO:0046332; F:SMAD binding; IDA:HGNC.
 GO:0005024; F:transforming growth factor beta-activated receptor activity; IEA:InterPro.
 GO:0007417; P:central nervous system development; IEA:Compara.
 GO:0046545; P:development of primary female sexual characteristics; IEA:Compara.
 GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:BHF-UCL.
 GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:HGNC.
 GO:0001942; P:hair follicle development; IEA:Compara.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0030308; P:negative regulation of cell growth; IDA:HGNC.
 GO:0038092; P:nodal signaling pathway; IGI:UniProtKB.
 GO:0018107; P:peptidyl-threonine phosphorylation; IDA:UniProtKB.
 GO:0032927; P:positive regulation of activin receptor signaling pathway; IDA:BHF-UCL.
 GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:HGNC.
 GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:1901165; P:positive regulation of trophoblast cell migration; IDA:BHF-UCL.
 GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IDA:HGNC. 
Interpro
 IPR000472; Activin_rcpt.
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR008271; Ser/Thr_kinase_AS.
 IPR003605; TGF_beta_rcpt_GS. 
Pfam
 PF01064; Activin_recp
 PF00069; Pkinase
 PF08515; TGF_beta_GS 
SMART
 SM00467; GS 
PROSITE
 PS51256; GS
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS