ACV1B_HUMAN - dbPTM
ACV1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACV1B_HUMAN
UniProt AC P36896
Protein Name Activin receptor type-1B
Gene Name ACVR1B
Organism Homo sapiens (Human).
Sequence Length 505
Subcellular Localization Cell membrane
Single-pass type I membrane protein.
Protein 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..
Protein Sequence MAESAGASSFFPLVVLLLAGSGGSGPRGVQALLCACTSCLQANYTCETDGACMVSIFNLDGMEHHVRTCIPKVELVPAGKPFYCLSSEDLRNTHCCYTDYCNRIDLRVPSGHLKEPEHPSMWGPVELVGIIAGPVFLLFLIIIIVFLVINYHQRVYHNRQRLDMEDPSCEMCLSKDKTLQDLVYDLSTSGSGSGLPLFVQRTVARTIVLQEIIGKGRFGEVWRGRWRGGDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTIEGMIKLALSAASGLAHLHMEIVGTQGKPGIAHRDLKSKNILVKKNGMCAIADLGLAVRHDAVTDTIDIAPNQRVGTKRYMAPEVLDETINMKHFDSFKCADIYALGLVYWEIARRCNSGGVHEEYQLPYYDLVPSDPSIEEMRKVVCDQKLRPNIPNWWQSYEALRVMGKMMRECWYANGAARLTALRIKKTLSQLSVQEDVKI
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 Orthologous
Protein Cluster
4Phosphorylation----MAESAGASSFF
----CCCCCCHHCCH		23.5926503514
24PhosphorylationLLAGSGGSGPRGVQA
HHHCCCCCCHHHHHH		49.5026503514
43N-linked_GlycosylationCTSCLQANYTCETDG
HHHHHHCCCEECCCC		21.49UniProtKB CARBOHYD
80 (in isoform 4)Ubiquitination-33.78-
80UbiquitinationVELVPAGKPFYCLSS
EEEECCCCCEEECCC		33.78-
156PhosphorylationINYHQRVYHNRQRLD
HHHHHHHHHCCCCCC		8.7946162389
163UbiquitinationYHNRQRLDMEDPSCE
HHCCCCCCCCCCCCH		40.3833845483
168PhosphorylationRLDMEDPSCEMCLSK
CCCCCCCCCHHHCCC		34.7223401153
174PhosphorylationPSCEMCLSKDKTLQD
CCCHHHCCCCCCHHH		33.6025841592
177UbiquitinationEMCLSKDKTLQDLVY
HHHCCCCCCHHHHCH		55.67-
184PhosphorylationKTLQDLVYDLSTSGS
CCHHHHCHHHHCCCC		20.61119605
206PhosphorylationVQRTVARTIVLQEII
EHHHHHHHHHHHHHH		13.00277944599
215UbiquitinationVLQEIIGKGRFGEVW
HHHHHHCCCCCCCHH		36.1833845483
215 (in isoform 4)Ubiquitination-36.18-
287UbiquitinationLVSDYHEHGSLFDYL
EEECCCCCCCHHHHH		20.1727667366
297PhosphorylationLFDYLNRYTVTIEGM
HHHHHHHEEEEHHHH		12.4222210691
298PhosphorylationFDYLNRYTVTIEGMI
HHHHHHEEEEHHHHH		14.1322210691
300PhosphorylationYLNRYTVTIEGMIKL
HHHHEEEEHHHHHHH		12.9122210691
328UbiquitinationEIVGTQGKPGIAHRD
EECCCCCCCCCCCCC		30.1927667366
339UbiquitinationAHRDLKSKNILVKKN
CCCCCCCCCEEEEEC		46.5527667366
341UbiquitinationRDLKSKNILVKKNGM
CCCCCCCEEEEECCE		5.5629967540
345UbiquitinationSKNILVKKNGMCAIA
CCCEEEEECCEEEEC		51.78-
380UbiquitinationQRVGTKRYMAPEVLD
CCCCCCCCCCHHHHH		10.1327667366
380PhosphorylationQRVGTKRYMAPEVLD
CCCCCCCCCCHHHHH		10.1314702039
386 (in isoform 4)Ubiquitination-4.73-
393UbiquitinationLDETINMKHFDSFKC
HHCCCCCCCCCCCCH		36.3129967540
434UbiquitinationQLPYYDLVPSDPSIE
ECCCCCCCCCCCCHH		3.7829967540
440UbiquitinationLVPSDPSIEEMRKVV
CCCCCCCHHHHHHHH		6.7332142685
463PhosphorylationIPNWWQSYEALRVMG
CCCHHHHHHHHHHHH		7.0725884760
486PhosphorylationANGAARLTALRIKKT
HCHHHHHHHHHHHHH		20.3524719451
492UbiquitinationLTALRIKKTLSQLSV
HHHHHHHHHHHHCCC		52.9432142685
527Phosphorylation-----------------------------
-----------------------------		24719451
533Ubiquitination-----------------------------------
-----------------------------------		32142685
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of ACV1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACV1B_HUMAN !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ACV1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMAD7_HUMANSMAD7physical
12023024
SMAD2_HUMANSMAD2physical
9892009
SMAD3_HUMANSMAD3physical
9892009
AVR2A_HUMANACVR2Aphysical
9892009
AVR2A_HUMANACVR2Aphysical
8612709
ACVR1_HUMANACVR1physical
8612709
FKB1A_HUMANFKBP1Aphysical
16720724
SMAD7_HUMANSMAD7physical
16720724
SMUF1_HUMANSMURF1physical
16720724
FKB1A_HUMANFKBP1Aphysical
15908921
T22D1_HUMANTSC22D1physical
21791611
NED4L_HUMANNEDD4Lphysical
19953087
IGSF1_HUMANIGSF1physical
11266516
SMUF1_HUMANSMURF1physical
12857866
BAMBI_HUMANBAMBIphysical
19758997
PEG10_HUMANPEG10physical
15611116
KAPCB_HUMANPRKACBphysical
21988832
BAG6_HUMANBAG6physical
21988832
OS9_HUMANOS9physical
21988832
RXRA_HUMANRXRAphysical
21988832
DOK1_MOUSEDok1physical
11927552
AVR2A_HUMANACVR2Aphysical
11927552
OTUB1_HUMANOTUB1physical
25872870
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00171Adenosine triphosphate
Regulatory Network of ACV1B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Identification of the phosphotyrosine proteome from thrombinactivated platelets.";
Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G.,Fitzgerald D.J.;
Proteomics 2:642-648(2002).
Cited for: PHOSPHORYLATION AT TYR-380.

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