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Protein

Phosphoinositide 3-kinase regulatory subunit 4

Gene

PIK3R4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20643123).1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mn2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531ATPPROSITE-ProRule annotation
Active sitei148 – 1481Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 409ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • cellular response to glucose starvation Source: UniProtKB
  • late endosome to vacuole transport Source: GO_Central
  • macroautophagy Source: GO_Central
  • pexophagy Source: GO_Central
  • phosphatidylinositol biosynthetic process Source: Reactome
  • positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • protein targeting to vacuole Source: GO_Central
  • receptor catabolic process Source: UniProtKB
  • regulation of cytokinesis Source: UniProtKB
  • toll-like receptor 9 signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS03788-MONOMER.
ReactomeiR-HSA-109704. PI3K Cascade.
R-HSA-1632852. Macroautophagy.
R-HSA-1660514. Synthesis of PIPs at the Golgi membrane.
R-HSA-1660516. Synthesis of PIPs at the early endosome membrane.
R-HSA-1660517. Synthesis of PIPs at the late endosome membrane.
R-HSA-168138. Toll Like Receptor 9 (TLR9) Cascade.
R-HSA-5668599. RHO GTPases Activate NADPH Oxidases.
SignaLinkiQ99570.
SIGNORiQ99570.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoinositide 3-kinase regulatory subunit 4 (EC:2.7.11.1)
Short name:
PI3-kinase regulatory subunit 4
Alternative name(s):
PI3-kinase p150 subunit
Phosphoinositide 3-kinase adaptor protein
Gene namesi
Name:PIK3R4
Synonyms:VPS151 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:8982. PIK3R4.

Subcellular locationi

  • Late endosome 1 Publication
  • Cytoplasmic vesicleautophagosome Curated
  • Membrane Curated; Lipid-anchor Curated

  • Note: 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).By similarityCurated

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33315.

Chemistry

ChEMBLiCHEMBL2189144.

Polymorphism and mutation databases

BioMutaiPIK3R4.
DMDMi74762700.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 13581357Phosphoinositide 3-kinase regulatory subunit 4PRO_0000086524Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine2 Publications
Modified residuei808 – 8081PhosphoserineCombined sources
Modified residuei813 – 8131PhosphoserineCombined sources
Modified residuei853 – 8531PhosphoserineCombined sources
Modified residuei865 – 8651PhosphoserineCombined sources
Modified residuei1316 – 13161PhosphothreonineCombined sources

Post-translational modificationi

Myristoylated.1 Publication
Probably autophosphorylated.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiQ99570.
MaxQBiQ99570.
PaxDbiQ99570.
PeptideAtlasiQ99570.
PRIDEiQ99570.

PTM databases

iPTMnetiQ99570.
PhosphoSiteiQ99570.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ99570.
CleanExiHS_PIK3R4.
ExpressionAtlasiQ99570. baseline and differential.
GenevisibleiQ99570. HS.

Organism-specific databases

HPAiHPA036032.
HPA036033.

Interactioni

Subunit structurei

Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex the core of which is composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 associating with additional regulatory/auxilliary subunits to form alternative complex forms. Alternative complex forms containing a forth regulatory subunit in a mutually exclusive manner are PI3K complex I (PI3KC3-C1) containing ATG14, and PI3K complex II (PI3KC3-C2) containing UVRAG (PubMed:8999962, PubMed:19270696, PubMed:23878393, PubMed:25490155). PI3KC3-C1 displays a V-shaped architecture with PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1 subcomplex (PubMed:25490155). Both, PI3KC3-C1 and PI3KC3-C2, can associate with further regulatory subunits, such as RUBCN, SH3GLB1/Bif-1, AMBRA1 and NRBF2 (PubMed:19270696, PubMed:20643123, PubMed:24785657). PI3KC3-C1 probably associates with PIK3CB (By similarity). Interacts with RAB7A in the presence of PIK3C3/VPS34 (PubMed:14617358). Interacts with NRBF2 (PubMed:24785657).By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NRBF2Q96F248EBI-1046979,EBI-2362014

Protein-protein interaction databases

BioGridi119059. 23 interactions.
DIPiDIP-42310N.
IntActiQ99570. 17 interactions.
MINTiMINT-1631706.
STRINGi9606.ENSP00000349205.

Chemistry

BindingDBiQ99570.

Structurei

3D structure databases

ProteinModelPortaliQ99570.
SMRiQ99570. Positions 26-168, 974-1234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 324299Protein kinasePROSITE-ProRule annotationAdd
BLAST
Repeati413 – 45038HEAT 1Add
BLAST
Repeati458 – 49538HEAT 2Add
BLAST
Repeati572 – 61039HEAT 3Add
BLAST
Repeati991 – 103040WD 1Add
BLAST
Repeati1040 – 107940WD 2Add
BLAST
Repeati1093 – 113442WD 3Add
BLAST
Repeati1139 – 117840WD 4Add
BLAST
Repeati1182 – 122342WD 5Add
BLAST
Repeati1237 – 127842WD 6Add
BLAST
Repeati1327 – 135832WD 7Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi781 – 7844Poly-Glu
Compositional biasi974 – 9774Poly-Pro

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 3 HEAT repeats.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG1240. Eukaryota.
ENOG410XPDN. LUCA.
GeneTreeiENSGT00390000016225.
HOGENOMiHOG000216566.
HOVERGENiHBG079542.
InParanoidiQ99570.
KOiK08333.
OMAiFQDIHHF.
OrthoDBiEOG7HMS08.
PhylomeDBiQ99570.
TreeFamiTF102034.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.130.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR021133. HEAT_type_2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
SM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF50978. SSF50978. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50077. HEAT_REPEAT. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99570-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNQLAGIAP SQILSVESYF SDIHDFEYDK SLGSTRFFKV ARAKHREGLV
60 70 80 90 100
VVKVFAIQDP TLPLTSYKQE LEELKIRLNS AQNCLPFQKA SEKASEKAAM
110 120 130 140 150
LFRQYVRDNL YDRISTRPFL NNIEKRWIAF QILTAVDQAH KSGVRHGDIK
160 170 180 190 200
TENVMVTSWN WVLLTDFASF KPTYLPEDNP ADFNYFFDTS RRRTCYIAPE
210 220 230 240 250
RFVDGGMFAT ELEYMRDPST PLVDLNSNQR TRGELKRAMD IFSAGCVIAE
260 270 280 290 300
LFTEGVPLFD LSQLLAYRNG HFFPEQVLNK IEDHSIRELV TQMIHREPDK
310 320 330 340 350
RLEAEDYLKQ QRGNAFPEIF YTFLQPYMAQ FAKETFLSAD ERILVIRKDL
360 370 380 390 400
GNIIHNLCGH DLPEKAEGEP KENGLVILVS VITSCLQTLK YCDSKLAALE
410 420 430 440 450
LILHLAPRLS VEILLDRITP YLLHFSNDSV PRVRAEALRT LTKVLALVKE
460 470 480 490 500
VPRNDINIYP EYILPGIAHL AQDDATIVRL AYAENIALLA ETALRFLELV
510 520 530 540 550
QLKNLNMEND PNNEEIDEVT HPNGNYDTEL QALHEMVQQK VVTLLSDPEN
560 570 580 590 600
IVKQTLMENG ITRLCVFFGR QKANDVLLSH MITFLNDKND WHLRGAFFDS
610 620 630 640 650
IVGVAAYVGW QSSSILKPLL QQGLSDAEEF VIVKALYALT CMCQLGLLQK
660 670 680 690 700
PHVYEFASDI APFLCHPNLW IRYGAVGFIT VVARQISTAD VYCKLMPYLD
710 720 730 740 750
PYITQPIIQI ERKLVLLSVL KEPVSRSIFD YALRSKDITS LFRHLHMRQK
760 770 780 790 800
KRNGSLPDCP PPEDPAIAQL LKKLLSQGMT EEEEDKLLAL KDFMMKSNKA
810 820 830 840 850
KANIVDQSHL HDSSQKGVID LAALGITGRQ VDLVKTKQEP DDKRARKHVK
860 870 880 890 900
QDSNVNEEWK SMFGSLDPPN MPQALPKGSD QEVIQTGKPP RSESSAGICV
910 920 930 940 950
PLSTSSQVPE VTTVQNKKPV IPVLSSTILP STYQIRITTC KTELQQLIQQ
960 970 980 990 1000
KREQCNAERI AKQMMENAEW ESKPPPPGWR PKGLLVAHLH EHKSAVNRIR
1010 1020 1030 1040 1050
VSDEHSLFAT CSNDGTVKIW NSQKMEGKTT TTRSILTYSR IGGRVKTLTF
1060 1070 1080 1090 1100
CQGSHYLAIA SDNGAVQLLG IEASKLPKSP KIHPLQSRIL DQKEDGCVVD
1110 1120 1130 1140 1150
MHHFNSGAQS VLAYATVNGS LVGWDLRSSS NAWTLKHDLK SGLITSFAVD
1160 1170 1180 1190 1200
IHQCWLCIGT SSGTMACWDM RFQLPISSHC HPSRARIRRL SMHPLYQSWV
1210 1220 1230 1240 1250
IAAVQGNNEV SMWDMETGDR RFTLWASSAP PLSELQPSPH SVHGIYCSPA
1260 1270 1280 1290 1300
DGNPILLTAG SDMKIRFWDL AYPERSYVVA GSTSSPSVSY YRKIIEGTEV
1310 1320 1330 1340 1350
VQEIQNKQKV GPSDDTPRRG PESLPVGHHD IITDVATFQT TQGFIVTASR

DGIVKVWK
Length:1,358
Mass (Da):153,103
Last modified:January 23, 2007 - v3
Checksum:i5B402175265B21F7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti342 – 3432RI → EK AA sequence (PubMed:8999962).Curated
Sequence conflicti553 – 5542KQ → FK AA sequence (PubMed:8999962).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti273 – 2731F → L.1 Publication
Corresponds to variant rs55951445 [ dbSNP | Ensembl ].
VAR_040997
Natural varianti342 – 3421R → H.1 Publication
Corresponds to variant rs56295394 [ dbSNP | Ensembl ].
VAR_040998
Natural varianti347 – 3471R → W.1 Publication
Corresponds to variant rs34797184 [ dbSNP | Ensembl ].
VAR_040999
Natural varianti388 – 3881T → I.1 Publication
Corresponds to variant rs34663155 [ dbSNP | Ensembl ].
VAR_041000
Natural varianti393 – 3931D → N.1 Publication
Corresponds to variant rs34633532 [ dbSNP | Ensembl ].
VAR_041001
Natural varianti699 – 6991L → V.1 Publication
Corresponds to variant rs56369596 [ dbSNP | Ensembl ].
VAR_041002
Natural varianti936 – 9361R → Q in a breast cancer sample; somatic mutation. 1 Publication
Corresponds to variant rs181132426 [ dbSNP | Ensembl ].
VAR_035632
Natural varianti1043 – 10431G → V.1 Publication
Corresponds to variant rs56160735 [ dbSNP | Ensembl ].
VAR_041003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08991 mRNA. Translation: CAA70176.1.
BC110318 mRNA. Translation: AAI10319.1.
BC127106 mRNA. Translation: AAI27107.1.
CCDSiCCDS3067.1.
RefSeqiNP_055417.1. NM_014602.2.
UniGeneiHs.149032.

Genome annotation databases

EnsembliENST00000356763; ENSP00000349205; ENSG00000196455.
GeneIDi30849.
KEGGihsa:30849.
UCSCiuc003enj.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08991 mRNA. Translation: CAA70176.1.
BC110318 mRNA. Translation: AAI10319.1.
BC127106 mRNA. Translation: AAI27107.1.
CCDSiCCDS3067.1.
RefSeqiNP_055417.1. NM_014602.2.
UniGeneiHs.149032.

3D structure databases

ProteinModelPortaliQ99570.
SMRiQ99570. Positions 26-168, 974-1234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119059. 23 interactions.
DIPiDIP-42310N.
IntActiQ99570. 17 interactions.
MINTiMINT-1631706.
STRINGi9606.ENSP00000349205.

Chemistry

BindingDBiQ99570.
ChEMBLiCHEMBL2189144.

PTM databases

iPTMnetiQ99570.
PhosphoSiteiQ99570.

Polymorphism and mutation databases

BioMutaiPIK3R4.
DMDMi74762700.

Proteomic databases

EPDiQ99570.
MaxQBiQ99570.
PaxDbiQ99570.
PeptideAtlasiQ99570.
PRIDEiQ99570.

Protocols and materials databases

DNASUi30849.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356763; ENSP00000349205; ENSG00000196455.
GeneIDi30849.
KEGGihsa:30849.
UCSCiuc003enj.4. human.

Organism-specific databases

CTDi30849.
GeneCardsiPIK3R4.
HGNCiHGNC:8982. PIK3R4.
HPAiHPA036032.
HPA036033.
MIMi602610. gene.
neXtProtiNX_Q99570.
PharmGKBiPA33315.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1240. Eukaryota.
ENOG410XPDN. LUCA.
GeneTreeiENSGT00390000016225.
HOGENOMiHOG000216566.
HOVERGENiHBG079542.
InParanoidiQ99570.
KOiK08333.
OMAiFQDIHHF.
OrthoDBiEOG7HMS08.
PhylomeDBiQ99570.
TreeFamiTF102034.

Enzyme and pathway databases

BioCyciMetaCyc:HS03788-MONOMER.
ReactomeiR-HSA-109704. PI3K Cascade.
R-HSA-1632852. Macroautophagy.
R-HSA-1660514. Synthesis of PIPs at the Golgi membrane.
R-HSA-1660516. Synthesis of PIPs at the early endosome membrane.
R-HSA-1660517. Synthesis of PIPs at the late endosome membrane.
R-HSA-168138. Toll Like Receptor 9 (TLR9) Cascade.
R-HSA-5668599. RHO GTPases Activate NADPH Oxidases.
SignaLinkiQ99570.
SIGNORiQ99570.

Miscellaneous databases

ChiTaRSiPIK3R4. human.
GeneWikiiPIK3R4.
GenomeRNAii30849.
PROiQ99570.
SOURCEiSearch...

Gene expression databases

BgeeiQ99570.
CleanExiHS_PIK3R4.
ExpressionAtlasiQ99570. baseline and differential.
GenevisibleiQ99570. HS.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.130.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR021133. HEAT_type_2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
SM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF50978. SSF50978. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50077. HEAT_REPEAT. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of p150, an adaptor protein for the human phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by phosphatidylinositol transfer protein to the p150.PtdIns 3-kinase complex."
    Panaretou C., Domin J., Cockcroft S., Waterfield M.D.
    J. Biol. Chem. 272:2477-2485(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 53-63; 333-343; 540-554 AND 786-791, MYRISTOYLATION AT GLY-2, PHOSPHORYLATION, COFACTOR, TISSUE SPECIFICITY, INTERACTION WITH PIK3C3.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Human VPS34 and p150 are Rab7 interacting partners."
    Stein M.P., Feng Y., Cooper K.L., Welford A.M., Wandinger-Ness A.
    Traffic 4:754-771(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB7A AND PIK3C3/VPS34, SUBCELLULAR LOCATION.
  4. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-808; SER-853 AND SER-865, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "A phosphatidylinositol 3-kinase class III sub-complex containing VPS15, VPS34, Beclin 1, UVRAG and BIF-1 regulates cytokinesis and degradative endocytic traffic."
    Thoresen S.B., Pedersen N.M., Liestol K., Stenmark H.
    Exp. Cell Res. 316:3368-3378(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  8. "Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages."
    Matsunaga K., Saitoh T., Tabata K., Omori H., Satoh T., Kurotori N., Maejima I., Shirahama-Noda K., Ichimura T., Isobe T., Akira S., Noda T., Yoshimori T.
    Nat. Cell Biol. 11:385-396(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BECN1; RUBCN; ATG14; PIK3C3 AND UVRAG.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  12. "Role of membrane association and Atg14-dependent phosphorylation in beclin-1-mediated autophagy."
    Fogel A.I., Dlouhy B.J., Wang C., Ryu S.W., Neutzner A., Hasson S.A., Sideris D.P., Abeliovich H., Youle R.J.
    Mol. Cell. Biol. 33:3675-3688(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BECN1.
  13. "NRBF2 regulates macroautophagy as a component of Vps34 Complex I."
    Cao Y., Wang Y., Abi Saab W.F., Yang F., Pessin J.E., Backer J.M.
    Biochem. J. 461:315-322(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NRBF2.
  14. "Architecture and dynamics of the autophagic phosphatidylinositol 3-kinase complex."
    Baskaran S., Carlson L.A., Stjepanovic G., Young L.N., Kim do J., Grob P., Stanley R.E., Nogales E., Hurley J.H.
    Elife 3:0-0(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECONSTITUTION OF THE PI3K COMPLEX I, ELECTRON MICROSCOPY OF THE PI3K COMPLEX I.
  15. "Global profiling of co- and post-translationally N-myristoylated proteomes in human cells."
    Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.
    Nat. Commun. 5:4919-4919(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
  16. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-936.
  17. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-273; HIS-342; TRP-347; ILE-388; ASN-393; VAL-699 AND VAL-1043.

Entry informationi

Entry nameiPI3R4_HUMAN
AccessioniPrimary (citable) accession number: Q99570
Secondary accession number(s): Q2TBF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.