Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q8K592

Entry ID Method Resolution Chain Position Source
AF-Q8K592-F1 Predicted AlphaFoldDB

52 variants for Q8K592

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389394908 6 G>R No EVA
rs231317987 13 A>V No EVA
rs3389388691 25 V>L No EVA
rs3389384769 33 R>L No EVA
rs3389400392 44 D>E No EVA
rs3389410377 60 C>R No EVA
rs3389403911 84 E>K No EVA
rs3389388752 105 T>I No EVA
rs214578882 124 P>L No EVA
rs3404943979 134 P>A No EVA
rs3406652399 134 P>R No EVA
rs3406732920 138 Q>L No EVA
rs3389364240 140 T>I No EVA
rs3406626994 163 I>N No EVA
rs3389392131 173 C>G No EVA
rs3389374174 182 E>* No EVA
rs3389374135 188 D>E No EVA
rs3389384783 196 L>Q No EVA
rs3389396845 203 Q>* No EVA
rs3389392096 208 G>E No EVA
rs3413084360 238 A>T No EVA
rs3400429667 251 D>G No EVA
rs3389384758 252 H>Q No EVA
rs3406652413 263 G>R No EVA
rs3406900690 263 G>V No EVA
rs3389387526 270 G>R No EVA
rs3389356591 276 E>* No EVA
rs3389387604 289 Q>K No EVA
rs3389396846 303 S>P No EVA
rs3389392068 309 A>S No EVA
rs3406652424 320 Q>L No EVA
rs3404944010 326 A>D No EVA
rs3389394929 341 R>S No EVA
rs3389384782 359 Q>H No EVA
rs3412852093 378 G>S No EVA
rs3389403928 400 A>S No EVA
rs3406627109 402 Q>* No EVA
rs3406563566 402 Q>R No EVA
rs3389392083 413 L>M No EVA
rs3389392102 422 D>V No EVA
rs3389400341 439 E>D No EVA
rs3389374132 492 L>R No EVA
rs244584750 508 H>Q No EVA
rs32514579 510 A>V No EVA
rs3389400324 516 S>N No EVA
rs3389310826 532 V>A No EVA
rs37779403 548 Q>H No EVA
rs3389410328 549 G>C No EVA
rs3389384735 554 S>I No EVA
rs250768767 560 D>A No EVA
rs3389394904 565 Y>F No EVA
rs3389356602 565 Y>H No EVA

No associated diseases with Q8K592

1 regional properties for Q8K592

Type Name Position InterPro Accession
domain Protein kinase domain 199 - 504 IPR000719

Functions

Description
EC Number 2.7.11.30 Protein-serine/threonine kinases
Subcellular Localization
  • Membrane ; Single-pass type I membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
activin receptor complex A protein complex that acts as an activin receptor. Heterodimeric activin receptors, comprising one Type I activin receptor and one Type II receptor polypeptide, and heterotrimeric receptors have been observed.
integral component of plasma membrane The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
receptor complex Any protein complex that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.

10 GO annotations of molecular function

Name Definition
activin binding Binding to activin, a dimer of inhibin-beta subunits.
activin receptor activity Combining with activin and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. Activin is one of two gonadal glycoproteins related to transforming growth factor beta.
anti-Mullerian hormone receptor activity Combining with anti-Mullerian hormone to initiate a change in cell activity.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
hormone binding Binding to an hormone, a naturally occurring substance secreted by specialized cells that affect the metabolism or behavior of cells possessing functional receptors for the hormone. Hormones may be produced by the same, or different, cell as express the receptor.
metal ion binding Binding to a metal ion.
protein homodimerization activity Binding to an identical protein to form a homodimer.
protein serine/threonine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
transforming growth factor beta receptor activity Combining with a transforming growth factor beta (TGFbeta) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity by catalysis of the reaction: ATP protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
transforming growth factor beta receptor activity, type II Combining with transforming growth factor beta to initiate a change in cell activity; upon ligand binding, binds to and catalyzes the phosphorylation of a type I TGF-beta receptor.

9 GO annotations of biological process

Name Definition
activin receptor signaling pathway The series of molecular signals initiated by an extracellular ligand binding to an activin receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription.
anti-Mullerian hormone signaling pathway The series of molecular signals initiated by the binding of anti-Mullerian hormone to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription.
cellular response to growth factor stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a growth factor stimulus.
female gonad development The process whose specific outcome is the progression of the female gonad over time, from its formation to the mature structure.
male gonad development The process whose specific outcome is the progression of the male gonad over time, from its formation to the mature structure.
pathway-restricted SMAD protein phosphorylation The process of introducing a phosphate group on to a pathway restricted SMAD protein. A pathway restricted SMAD protein is an effector protein that acts directly downstream of the transforming growth factor family receptor.
protein phosphorylation The process of introducing a phosphate group on to a protein.
sex differentiation The establishment of the sex of an organism by physical differentiation.
transforming growth factor beta receptor signaling pathway The series of molecular signals initiated by an extracellular ligand binding to a transforming growth factor beta receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription.

15 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q95126 ACVR2B Activin receptor type-2B Bos taurus (Bovine) PR
Q90670 ACVR2B Activin receptor type-2B Gallus gallus (Chicken) PR
Q90999 TGFBR2 TGF-beta receptor type-2 Gallus gallus (Chicken) PR
Q13705 ACVR2B Activin receptor type-2B Homo sapiens (Human) PR
P37173 TGFBR2 TGF-beta receptor type-2 Homo sapiens (Human) PR
Q61288 Acvrl1 Serine/threonine-protein kinase receptor R3 Mus musculus (Mouse) PR
Q8K348 Acvr1c Activin receptor type-1C Mus musculus (Mouse) PR
Q62312 Tgfbr2 TGF-beta receptor type-2 Mus musculus (Mouse) PR
P27040 Acvr2b Activin receptor type-2B Mus musculus (Mouse) PR
Q64729 Tgfbr1 TGF-beta receptor type-1 Mus musculus (Mouse) PR
Q66T47 ACVR2B Activin receptor type-2B Sus scrofa (Pig) PR
P38445 Acvr2b Activin receptor type-2B Rattus norvegicus (Rat) PR
P38438 Tgfbr2 TGF-beta receptor type-2 Rattus norvegicus (Rat) PR
Q62893 Amhr2 Anti-Muellerian hormone type-2 receptor Rattus norvegicus (Rat) PR
P50488 daf-4 Cell surface receptor daf-4 Caenorhabditis elegans PR
10 20 30 40 50 60
MLGTLGLWTL LPAAAQVSPN RRTCVFFEAP GVRGSTKTLG EMVDAGPGPP KGIRCLYSHC
70 80 90 100 110 120
CFGIWNLTHG RAQVEMQGCR DSDEPGCESL HCDPVPRAHP NPSSTLFTCS CGTDFCNANY
130 140 150 160 170 180
SHLPPSGNQG APGPQEPQAT PGGPVWMALL LLGMFLVLLL SSIILALLQR KACRVQGGSD
190 200 210 220 230 240
PEPGSGGDCS EELPELAELR FSQVIQEGGH AVVWAGRLQG EMVAIKAFPP RAVAQFRAER
250 260 270 280 290 300
AVYQLLGLQH DHIVRFITAG QGGPGPLPSG PLLVLELYPK GSLCHYLTQY TSDWGSSLRM
310 320 330 340 350 360
ALSLAEGLAF LHEERWQDGQ YKPGIAHRDL SSQNVLIRED RSCAIGDLGL ALVLPGLAQP
370 380 390 400 410 420
PALAPTQPRG PAAILEAGTQ RYMAPELLDK TLDLQDWGTA LQRADVYSLA LLLWEILSRC
430 440 450 460 470 480
SDLRPDHRPP PFQLAYEAEL GSNPSACELW ALAVEERKRP NIPSTWSCSA TDPRGLRELL
490 500 510 520 530 540
EDCWDADPEA RLTAECVQQR LAALAYPHGA SSFPESPQGC PENCLSAPAS AVFPCRPQQS
550 560
SCLLSVQQGP GSRSPDPVGD TVQVYVNE