Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00276
Entry Name
UniProt Accession
Theoretical PI
6.74
Molecular Weight
153103.47
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Phosphoinositide 3-kinase regulatory subunit 4
Protein Synonyms/Alias
PI3-kinase regulatory subunit 4; 2.7.11.1; PI3-kinase p150 subunit; Phosphoinositide 3-kinase adaptor protein;
Gene Name
PIK3R4
Gene Synonyms/Alias
Created Date
06-DEC-2005
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGNQLAGIA
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Panaretou C, Domin J, Cockcroft S, Waterfield MD. Characterization of p150, anadaptor protein for the human phosphatidylinositol (PtdIns) 3-kinase. Substratepresentation by phosphatidylinositol transfer protein to the p150.Ptdins 3-kinasecomplex. J Biol Chem. 1997 Jan 24;272(4):2477-85.[PMID:8999962]
Functional Description
Regulatory subunit of the PI3K complex. May regulate membrane trafficking late in the endocytic pathway.
Sequence Annotation
Domain: 26 324 Protein kinase.
Nucleotide-binding: 32 40 ATP.
Active site: 148 148 Proton acceptor.
Binding site: 53 53 ATP.
Modified residue: 808 808 Phosphoserine.
Modified residue: 853 853 Phosphoserine.
Modified residue: 865 865 Phosphoserine.
Modified residue: 1316 1316 Phosphothreonine.
Protein Length
1358 AA.
Protein Sequence
(Canonical)
MGNQLAGIAP SQILSVESYF SDIHDFEYDK SLGSTRFFKV ARAKHREGLV VVKVFAIQDP  60
TLPLTSYKQE LEELKIRLNS AQNCLPFQKA SEKASEKAAM LFRQYVRDNL YDRISTRPFL  120
NNIEKRWIAF QILTAVDQAH KSGVRHGDIK TENVMVTSWN WVLLTDFASF KPTYLPEDNP  180
ADFNYFFDTS RRRTCYIAPE RFVDGGMFAT ELEYMRDPST PLVDLNSNQR TRGELKRAMD  240
IFSAGCVIAE LFTEGVPLFD LSQLLAYRNG HFFPEQVLNK IEDHSIRELV TQMIHREPDK  300
RLEAEDYLKQ QRGNAFPEIF YTFLQPYMAQ FAKETFLSAD ERILVIRKDL GNIIHNLCGH  360
DLPEKAEGEP KENGLVILVS VITSCLQTLK YCDSKLAALE LILHLAPRLS VEILLDRITP  420
YLLHFSNDSV PRVRAEALRT LTKVLALVKE VPRNDINIYP EYILPGIAHL AQDDATIVRL  480
AYAENIALLA ETALRFLELV QLKNLNMEND PNNEEIDEVT HPNGNYDTEL QALHEMVQQK  540
VVTLLSDPEN IVKQTLMENG ITRLCVFFGR QKANDVLLSH MITFLNDKND WHLRGAFFDS  600
IVGVAAYVGW QSSSILKPLL QQGLSDAEEF VIVKALYALT CMCQLGLLQK PHVYEFASDI  660
APFLCHPNLW IRYGAVGFIT VVARQISTAD VYCKLMPYLD PYITQPIIQI ERKLVLLSVL  720
KEPVSRSIFD YALRSKDITS LFRHLHMRQK KRNGSLPDCP PPEDPAIAQL LKKLLSQGMT  780
EEEEDKLLAL KDFMMKSNKA KANIVDQSHL HDSSQKGVID LAALGITGRQ VDLVKTKQEP  840
DDKRARKHVK QDSNVNEEWK SMFGSLDPPN MPQALPKGSD QEVIQTGKPP RSESSAGICV  900
PLSTSSQVPE VTTVQNKKPV IPVLSSTILP STYQIRITTC KTELQQLIQQ KREQCNAERI  960
AKQMMENAEW ESKPPPPGWR PKGLLVAHLH EHKSAVNRIR VSDEHSLFAT CSNDGTVKIW  1020
NSQKMEGKTT TTRSILTYSR IGGRVKTLTF CQGSHYLAIA SDNGAVQLLG IEASKLPKSP  1080
KIHPLQSRIL DQKEDGCVVD MHHFNSGAQS VLAYATVNGS LVGWDLRSSS NAWTLKHDLK  1140
SGLITSFAVD IHQCWLCIGT SSGTMACWDM RFQLPISSHC HPSRARIRRL SMHPLYQSWV  1200
IAAVQGNNEV SMWDMETGDR RFTLWASSAP PLSELQPSPH SVHGIYCSPA DGNPILLTAG  1260
SDMKIRFWDL AYPERSYVVA GSTSSPSVSY YRKIIEGTEV VQEIQNKQKV GPSDDTPRRG  1320
PESLPVGHHD IITDVATFQT TQGFIVTASR DGIVKVWK                          1358
FASTA
(Canonical)
>LipidDB-9606-00276|Q99570
MGNQLAGIAPSQILSVESYFSDIHDFEYDKSLGSTRFFKVARAKHREGLVVVKVFAIQDP
TLPLTSYKQELEELKIRLNSAQNCLPFQKASEKASEKAAMLFRQYVRDNLYDRISTRPFL
NNIEKRWIAFQILTAVDQAHKSGVRHGDIKTENVMVTSWNWVLLTDFASFKPTYLPEDNP
ADFNYFFDTSRRRTCYIAPERFVDGGMFATELEYMRDPSTPLVDLNSNQRTRGELKRAMD
IFSAGCVIAELFTEGVPLFDLSQLLAYRNGHFFPEQVLNKIEDHSIRELVTQMIHREPDK
RLEAEDYLKQQRGNAFPEIFYTFLQPYMAQFAKETFLSADERILVIRKDLGNIIHNLCGH
DLPEKAEGEPKENGLVILVSVITSCLQTLKYCDSKLAALELILHLAPRLSVEILLDRITP
YLLHFSNDSVPRVRAEALRTLTKVLALVKEVPRNDINIYPEYILPGIAHLAQDDATIVRL
AYAENIALLAETALRFLELVQLKNLNMENDPNNEEIDEVTHPNGNYDTELQALHEMVQQK
VVTLLSDPENIVKQTLMENGITRLCVFFGRQKANDVLLSHMITFLNDKNDWHLRGAFFDS
IVGVAAYVGWQSSSILKPLLQQGLSDAEEFVIVKALYALTCMCQLGLLQKPHVYEFASDI
APFLCHPNLWIRYGAVGFITVVARQISTADVYCKLMPYLDPYITQPIIQIERKLVLLSVL
KEPVSRSIFDYALRSKDITSLFRHLHMRQKKRNGSLPDCPPPEDPAIAQLLKKLLSQGMT
EEEEDKLLALKDFMMKSNKAKANIVDQSHLHDSSQKGVIDLAALGITGRQVDLVKTKQEP
DDKRARKHVKQDSNVNEEWKSMFGSLDPPNMPQALPKGSDQEVIQTGKPPRSESSAGICV
PLSTSSQVPEVTTVQNKKPVIPVLSSTILPSTYQIRITTCKTELQQLIQQKREQCNAERI
AKQMMENAEWESKPPPPGWRPKGLLVAHLHEHKSAVNRIRVSDEHSLFATCSNDGTVKIW
NSQKMEGKTTTTRSILTYSRIGGRVKTLTFCQGSHYLAIASDNGAVQLLGIEASKLPKSP
KIHPLQSRILDQKEDGCVVDMHHFNSGAQSVLAYATVNGSLVGWDLRSSSNAWTLKHDLK
SGLITSFAVDIHQCWLCIGTSSGTMACWDMRFQLPISSHCHPSRARIRRLSMHPLYQSWV
IAAVQGNNEVSMWDMETGDRRFTLWASSAPPLSELQPSPHSVHGIYCSPADGNPILLTAG
SDMKIRFWDLAYPERSYVVAGSTSSPSVSYYRKIIEGTEVVQEIQNKQKVGPSDDTPRRG
PESLPVGHHDIITDVATFQTTQGFIVTASRDGIVKVWK
Gene Ontology
GO:0005930; C:axoneme; ISS:UniProtKB
GO:0005829; C:cytosol; TAS:Reactome
GO:0005770; C:late endosome; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProtKB
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0004672; F:protein kinase activity; NAS:UniProtKB
GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW
GO:0045087; P:innate immune response; TAS:Reactome
GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome
GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome
GO:0006644; P:phospholipid metabolic process; TAS:Reactome
GO:0006468; P:protein phosphorylation; NAS:UniProtKB
GO:0044281; P:small molecule metabolic process; TAS:Reactome
GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome
GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome
Interpro
InterPro; IPR011989; ARM-like
InterPro; IPR016024; ARM-type_fold
InterPro; IPR021133; HEAT_type_2
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR008271; Ser/Thr_kinase_AS
InterPro; IPR015943; WD40/YVTN_repeat-like_dom
InterPro; IPR001680; WD40_repeat
InterPro; IPR019775; WD40_repeat_CS
InterPro; IPR017986; WD40_repeat_dom
Pfam
Pfam; PF00069; Pkinase;
Pfam; PF00400; WD40;
SMART
SMART; SM00320; WD40;
PROSITE
PROSITE; PS50077; HEAT_REPEAT;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00108; PROTEIN_KINASE_ST;
PROSITE; PS00678; WD_REPEATS_1;
PROSITE; PS50082; WD_REPEATS_2;
PROSITE; PS50294; WD_REPEATS_REGION;
PRINTS