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

157-179 (Activation loop from InterPro)

Target domain

9-271 (Protein kinase domain)

Relief mechanism

Assay

Autoinhibited structure

Activated structure

1 structures for Q9QY01

Entry ID Method Resolution Chain Position Source
AF-Q9QY01-F1 Predicted AlphaFoldDB

24 variants for Q9QY01

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389163660 113 H>Y No EVA
rs3389135886 123 H>Q No EVA
rs3389151904 167 S>I No EVA
rs3389140128 205 Y>H No EVA
rs3401714462 236 I>V No EVA
rs3389168273 274 V>I No EVA
rs3389177469 356 V>D No EVA
rs3389163305 420 T>S No EVA
rs3389128656 453 S>F No EVA
rs26955148 501 A>D No EVA
rs3389171994 528 S>N No EVA
rs3389159212 569 G>D No EVA
rs225859317 629 A>P No EVA
rs3402365619 649 Q>L No EVA
rs3389168313 731 P>S No EVA
rs3389128672 734 S>G No EVA
rs3389166302 768 V>I No EVA
rs3389140144 770 V>L No EVA
rs3389168304 784 G>VSDG* No EVA
rs241044052 787 G>A No EVA
rs3389102655 788 A>V No EVA
rs3389140079 807 I>V No EVA
rs3389171980 818 T>K No EVA
rs263131109 944 N>S No EVA

No associated diseases with Q9QY01

3 regional properties for Q9QY01

Type Name Position InterPro Accession
domain SET domain 493 - 643 IPR001214
domain SRA-YDG 200 - 356 IPR003105
domain Pre-SET domain 384 - 490 IPR007728

Functions

Description
EC Number 2.7.11.1 Protein-serine/threonine kinases
Subcellular Localization
  • Cytoplasmic vesicle membrane ; Peripheral membrane protein
  • Localizes to pre-autophagosomal membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoplasmic vesicle membrane The lipid bilayer surrounding a cytoplasmic vesicle.
phagophore assembly site membrane A cellular membrane associated with the phagophore assembly site.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
protein serine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate.
protein serine/threonine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.

14 GO annotations of biological process

Name Definition
autophagosome assembly The formation of a double membrane-bounded structure, the autophagosome, that occurs when a specialized membrane sac, called the isolation membrane, starts to enclose a portion of the cytoplasm.
autophagy The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation.
autophagy of mitochondrion The autophagic process in which mitochondria are delivered to a type of vacuole and degraded in response to changing cellular conditions.
axon extension Long distance growth of a single axon process involved in cellular development.
collateral sprouting The process in which outgrowths develop from the shafts of existing axons.
late nucleophagy A type of nucleophagy, distinct from piecemeal microautophagy of the nucleus (PNM) where the nuclear material is delivered to the vacuole/lysosome for breakdown and recycling later than observed for PNM.
negative regulation of collateral sprouting Any process that stops, prevents, or reduces the frequency, rate or extent of collateral sprouting.
peptidyl-serine phosphorylation The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine.
piecemeal microautophagy of the nucleus Degradation of a cell nucleus by lysosomal microautophagy.
positive regulation of autophagy Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.
protein autophosphorylation The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
response to starvation Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of nourishment.
reticulophagy The selective autohagy process in which parts of the endoplasmic reticulum are loaded into autophagosomes, delivered to the vacuole, and degraded in response to changing cellular conditions.
signal transduction The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P53104 ATG1 Serine/threonine-protein kinase ATG1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q6PHR2 ULK3 Serine/threonine-protein kinase ULK3 Homo sapiens (Human) PR
Q3U3Q1 Ulk3 Serine/threonine-protein kinase ULK3 Mus musculus (Mouse) PR
10 20 30 40 50 60
MEVVGDFEYC KRDLVGHGAF AVVFRGRHRQ KTDWEVAIKS INKKNLSKSQ ILLGKEIKIL
70 80 90 100 110 120
KELQHENIVA LYDVQELPNS VFLVMEYCNG GDLADYLQAK GTLSEDTIRV FLHQIAAAMR
130 140 150 160 170 180
ILHSKGIIHR DLKPQNILLS YANRRKSNVS GIRIKIADFG FARYLHSNTM AATLCGSPMY
190 200 210 220 230 240
MAPEVIMSQH YDAKADLWSI GTVIYQCLVG KPPFQANSPQ DLRMFYEKNR SLMPSIPRET
250 260 270 280 290 300
SPYLANLLLG LLQRNQKDRM DFEAFFSHPF LEQVPVKKSC PVPVPVYSGP VPGSSCSSSP
310 320 330 340 350 360
SCRFASPPSL PDMQHIQEEN LSSPPLGPPN YLQVSKDSAS NSSKNSSCDT DDFVLVPHNI
370 380 390 400 410 420
SSDHSYDMPM GTTARRASNE FFMCGGQCQP TVSPHSETAP IPVPTQVRNY QRIEQNLIST
430 440 450 460 470 480
ASSGTNPHGS PRSAVVRRSN TSPMGFLRVG SCSPVPGDTV QTGGRRLSTG SSRPYSPSPL
490 500 510 520 530 540
VGTIPEQFSQ CCCGHPQGHE ARSRHSSGSP VPQTQAPQSL LLGARLQSAP TLTDIYQNKQ
550 560 570 580 590 600
KLRKQHSDPV CPSHAGAGYS YSPQPSRPGS LGTSPTKHTG SSPRNSDWFF KTPLPTIIGS
610 620 630 640 650 660
PTKTTAPFKI PKTQASSNLL ALVTRHGPAE SQSKDGNDPR ECSHCLSVQG SERHRSEQQQ
670 680 690 700 710 720
SKAVFGRSVS TGKLSEQQVK APLGGHQGST DSLNTERPMD VAPAGACGVM LALPAGTAAS
730 740 750 760 770 780
ARAVLFTVGS PPHSATAPTC THMVLRTRTT SVGSSSSGGS LCSASGRVCV GSPPGPGLGS
790 800 810 820 830 840
SPPGAEGAPS LRYVPYGASP PSLEGLITFE APELPEETLM EREHTDTLRH LNMMLMFTEC
850 860 870 880 890 900
VLDLTAVRGG NPELCTSAVS LYQIQESVVV DQISQLSKDW GRVEQLVLYM KAAQLLAASL
910 920 930 940 950 960
HLAKAQVKSG KLSPSMAVKQ VVKNLNERYK FCITMCKKLT EKLNRFFSDK QRFIDEINSV
970 980 990 1000 1010 1020
TAEKLIYNCA VEMVQSAALD EMFQQTEDIV YRYHKAALLL EGLSKILQDP TDVENVHKYK
1030
CSIERRLSAL CCSTATV