AVR2B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AVR2B_HUMAN
• UniProt AC: Q13705
• Protein Name: Activin receptor type-2B
• Gene Name: ACVR2B
• Organism: Homo sapiens (Human).
• Sequence Length: 512
• Subcellular Localization: Cell membrane; Single-pass type I membrane protein.
• Protein Description: Transmembrane serine/threonine kinase activin type-2 receptor 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 Sequence: MTAPWVALALLWGSLCAGSGRGEAETRECIYYNANWELERTNQSGLERCEGEQDKRLHCYASWRNSSGTIELVKKGCWLDDFNCYDRQECVATEENPQVYFCCCEGNFCNERFTHLPEAGGPEVTYEPPPTAPTLLTVLAYSLLPIGGLSLIVLLAFWMYRHRKPPYGHVDIHEDPGPPPPSPLVGLKPLQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEVELWLITAFHDKGSLTDYLKGNIITWNELCHVAETMSRGLSYLHEDVPWCRGEGHKPSIAHRDFKSKNVLLKSDLTAVLADFGLAVRFEPGKPPGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQHPSLEELQEVVVHKKMRPTIKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERVSLIRRSVNGTTSDCLVSLVTSVTNVDLPPKESSI

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	ALALLWGSLCAGSGR HHHHHHHHHHCCCCC	14.53	25348772
19	Phosphorylation	WGSLCAGSGRGEAET HHHHHCCCCCCHHHH	13.54	63650545
42	N-linked_Glycosylation	NWELERTNQSGLERC CCEEEECCCCCHHCC	40.00	22718755
65	N-linked_Glycosylation	HCYASWRNSSGTIEL EEEEEEECCCCCEEE	33.98	22718755
224	Ubiquitination	KIFPLQDKQSWQSER EEEECCCHHCHHHHH	33.02	29967540
240	Ubiquitination	IFSTPGMKHENLLQF HHCCCCCCHHHHHHH	54.40	29967540
325	Ubiquitination	AHRDFKSKNVLLKSD CCCCCCCCCEEEHHH	52.22	-
488	Phosphorylation	IRRSVNGTTSDCLVS HHHHCCCCHHHHHHH	20.23	50563359
490	Phosphorylation	RSVNGTTSDCLVSLV HHCCCCHHHHHHHHH	26.60	46158821

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of AVR2B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AVR2B_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of AVR2B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACV1B_HUMAN	ACVR1B	physical	8622651
GDF5_HUMAN	GDF5	physical	8702914
BMP6_HUMAN	BMP6	physical	10504300
GDF8_HUMAN	MSTN	physical	11459935
ACV1B_HUMAN	ACVR1B	physical	8612709
IGSF1_HUMAN	IGSF1	physical	11266516
SMAD2_HUMAN	SMAD2	physical	11094085
PEG10_HUMAN	PEG10	physical	15611116
INHBA_HUMAN	INHBA	physical	8242742
GDF2_HUMAN	GDF2	physical	22718755
BMP10_HUMAN	BMP10	physical	22718755

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.