Q5R9I3

PR
Gene name
PIK3R4
Protein name
Phosphoinositide 3-kinase regulatory subunit 4
Names
PI3-kinase regulatory subunit 4
Species
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
KEGG Pathway
pon:100172860
EC number
2.7.11.1: Protein-serine/threonine kinases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

806-942 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

165-195 (Activation loop from InterPro)

Target domain

26-324 (Protein kinase domain)

Relief mechanism

Assay

References

Autoinhibited structure

Activated structure

1 structures for Q5R9I3

Entry ID Method Resolution Chain Position Source
AF-Q5R9I3-F1 Predicted AlphaFoldDB

No variants for Q5R9I3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5R9I3

No associated diseases with Q5R9I3

9 regional properties for Q5R9I3

Type Name Position InterPro Accession
domain Protein kinase domain 26 - 324 IPR000719
repeat WD40 repeat 982 - 1030 IPR001680-1
repeat WD40 repeat 1031 - 1070 IPR001680-2
repeat WD40 repeat 1132 - 1169 IPR001680-3
repeat WD40 repeat 1171 - 1214 IPR001680-4
repeat WD40 repeat 1228 - 1269 IPR001680-5
repeat WD40 repeat 1317 - 1358 IPR001680-6
active_site Serine/threonine-protein kinase, active site 144 - 156 IPR008271
repeat HEAT, type 2 463 - 493 IPR021133

Functions

Description
EC Number 2.7.11.1 Protein-serine/threonine kinases
Subcellular Localization
  • Late endosome
  • Cytoplasmic vesicle, autophagosome
  • Membrane ; Lipid-anchor
  • As component of the PI3K complex I localized to pre-autophagosome structures
  • As component of the PI3K complex II localized predominantly to endosomes
  • Localizes also to discrete punctae along the ciliary axoneme (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
autophagosome A double-membrane-bounded compartment that engulfs endogenous cellular material as well as invading microorganisms to target them to the lytic vacuole/lysosome for degradation as part of macroautophagy.
axoneme The bundle of microtubules and associated proteins that forms the core of cilia (also called flagella) in eukaryotic cells and is responsible for their movements.
late endosome A prelysosomal endocytic organelle differentiated from early endosomes by lower lumenal pH and different protein composition. Late endosomes are more spherical than early endosomes and are mostly juxtanuclear, being concentrated near the microtubule organizing center.
phosphatidylinositol 3-kinase complex, class III A phosphatidylinositol 3-kinase complex that contains a catalytic class III phosphoinositide 3-kinase (PI3K) subunit bound to a regulatory (adaptor) subunit. Additional adaptor proteins may be present. Class III PI3Ks have a substrate specificity restricted to phosphatidylinositol (PI).

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.

4 GO annotations of biological process

Name Definition
cellular response to glucose starvation 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 deprivation of glucose.
late endosome to vacuole transport The directed movement of substances from late endosomes to the vacuole. In yeast, after transport to the prevacuolar compartment, endocytic content is delivered to the late endosome and on to the vacuole. This pathway is analogous to endosome to lysosome transport.
macroautophagy The major inducible pathway for the general turnover of cytoplasmic constituents in eukaryotic cells, it is also responsible for the degradation of active cytoplasmic enzymes and organelles during nutrient starvation. Macroautophagy involves the formation of double-membrane-bounded autophagosomes which enclose the cytoplasmic constituent targeted for degradation in a membrane-bounded structure. Autophagosomes then fuse with a lysosome (or vacuole) releasing single-membrane-bounded autophagic bodies that are then degraded within the lysosome (or vacuole). Some types of macroautophagy, e.g. pexophagy, mitophagy, involve selective targeting of the targets to be degraded.
protein phosphorylation The process of introducing a phosphate group on to a protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGNQLAGIAP SQILSVESYF SDIHDFEYDK SLGSTRFFKV ARAKHREGLV VVKVFAIQDP
70 80 90 100 110 120
TLPLTSYKQE LEELKIRLNS AQNCLPFQKA SEKASEKAAM LFRQYVRDNL YDRISTRPFL
130 140 150 160 170 180
NNIENRWIAF QILTAVDQAH KPGVRHGDIK TENVMVTSWN WVLLTDFASF KPTYLPEDNP
190 200 210 220 230 240
ADFNYFFDTS RRRTCYIAPE RFVDGGMFAT ELEYMRDPST PLVDLNSNQR TRGELKRAMD
250 260 270 280 290 300
IFSAGCVIAE LFTEGVPLFD LSQLLAYRNG HFFPEQVLNK IEDHSIRELV TQMIHREPDK
310 320 330 340 350 360
RLEAEDYLKQ QRGNAFPEIF YTFLQPYMAQ FAKETFLSAD ERILVIRKDL GNIIHNLCGH
370 380 390 400 410 420
DLPEKTEEEP KENGLVILVS VITSCLQTLK YYDSKLAALE LILHLAPRLG VEILLDRITP
430 440 450 460 470 480
YLLHFSNDSV PRVRAEALRT LTKVLALVKE VPRNDINIYP EYILPGIAHL AQDDATIVRL
490 500 510 520 530 540
AYAENIALLA ETALRFLELV QLKNLNMEND PNNEEIDEVT HPNGNYDTEL QALHEMVQQK
550 560 570 580 590 600
VVTLLSDPEN IVKQTLMENG ITRLCVFFGR QKANDVLLSH MITFLNDKND WHLRGAFFDS
610 620 630 640 650 660
IVGVAAYVGW QSSSILKPLL QQGLSDAEEF VIVKALYALT CMCQLGLLQK PHVYEFASDI
670 680 690 700 710 720
APFLCHPNLW IRYGAVGFVT VVARQISTAD VYCKLMPYLD PYITQPIIQI ERKLVLLSVL
730 740 750 760 770 780
KEPVSRSIFD YALRSKDITS LFRHLHMRQK KRNGSLPDCP PPEDPAIAQL LKKLLSQGMT
790 800 810 820 830 840
EDEEDKLLAL KDFMMKSNKA KANIVDQSHL HDSSQKGVID LAALGITGRQ VDLVKTKQEP
850 860 870 880 890 900
DDKRARKHVK QDSNVNEEWK SMFGSLDPPN MPQALPKGSD QEVIQTGKPP RSESSAGICV
910 920 930 940 950 960
PLSTSPQVPE VTTIQNKKPV IPVLSSTILP STYQIRITTC KTELQQLIQQ KREQCNAERI
970 980 990 1000 1010 1020
AKQMMENAEW ESKPPPPGWR PKGLLVAHLH EHKSAVNRIR VSDEHSLFAT CSNDGTVKIR
1030 1040 1050 1060 1070 1080
NSQKMEGKTT TTRSILTYSR VGGRVKTLTF CQGSHYLAIA SDNGAVQLLG IEASKLPKSP
1090 1100 1110 1120 1130 1140
KIHPLQSRIL DQKEDGCVVD MHHFNSGAQS VLAYATVNGS LVGWDLRSSS NAWTLKHDLK
1150 1160 1170 1180 1190 1200
SGLITSFAVD IHQCWLCIGT SSGTMACWDM RFQLPISSHC HPSRARIRRL SMHPLYQSWV
1210 1220 1230 1240 1250 1260
IAAVQGNNEV SMWDMETGDR RFTLWASSAP PLSELQPSPH SVHGIYCSPA DGNPILLTAG
1270 1280 1290 1300 1310 1320
SDMKIRFWDL AYPERSYVVA GSTSSPSVSY YRKIIEGTEV VQEIQNKQKV GPSDDTPRRG
1330 1340 1350
PESLPVGHHD IITDVATFQT TQGFIVTASR DGIVKVWK