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Protein

Phosphatidylinositol 3-kinase catalytic subunit type 3

Gene

PIK3C3

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

Functioni

Catalytic 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 required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20643123, PubMed:20208530). Involved in the transport of lysosomal enzyme precursors to lysosomes. Required for transport from early to late endosomes (By similarity).By similarityCurated4 Publications

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate.

Cofactori

Mn2+1 Publication

GO - Molecular functioni

  • 1-phosphatidylinositol-3-kinase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: MGI
  • protein kinase activity Source: Ensembl

GO - Biological processi

  • autophagy Source: MGI
  • cellular response to glucose starvation Source: UniProtKB
  • cytokinesis Source: UniProtKB
  • early endosome to late endosome transport Source: UniProtKB
  • endosome organization Source: Ensembl
  • macroautophagy Source: UniProtKB
  • phosphatidylinositol biosynthetic process Source: Reactome
  • phosphatidylinositol-mediated signaling Source: Ensembl
  • protein lipidation Source: MGI
  • protein localization to pre-autophagosomal structure Source: Ensembl
  • protein processing Source: Ensembl
  • regulation of cytokinesis Source: UniProtKB
  • regulation of protein secretion Source: Ensembl
  • response to leucine Source: Ensembl
  • toll-like receptor 9 signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Autophagy, Cell cycle, Cell division

Keywords - Ligandi

ATP-binding, Manganese, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS01275-MONOMER.
ZFISH:HS01275-MONOMER.
BRENDAi2.7.1.137. 2681.
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.
SIGNORiQ8NEB9.

Chemistry databases

SwissLipidsiSLP:000000904.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 3-kinase catalytic subunit type 3 (EC:2.7.1.137)
Short name:
PI3-kinase type 3
Short name:
PI3K type 3
Short name:
PtdIns-3-kinase type 3
Alternative name(s):
Phosphatidylinositol 3-kinase p100 subunit
Phosphoinositide-3-kinase class 3
hVps34
Gene namesi
Name:PIK3C3
Synonyms:VPS34
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:8974. PIK3C3.

Subcellular locationi

GO - Cellular componenti

  • autolysosome Source: MGI
  • axoneme Source: UniProtKB
  • cytosol Source: Reactome
  • late endosome Source: UniProtKB
  • membrane Source: UniProtKB
  • midbody Source: UniProtKB
  • phagocytic vesicle membrane Source: Reactome
  • phosphatidylinositol 3-kinase complex Source: GO_Central
  • phosphatidylinositol 3-kinase complex, class III Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5289.
OpenTargetsiENSG00000078142.
PharmGKBiPA33307.

Chemistry databases

ChEMBLiCHEMBL1075165.
GuidetoPHARMACOLOGYi2152.

Polymorphism and mutation databases

BioMutaiPIK3C3.
DMDMi74730233.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000888021 – 887Phosphatidylinositol 3-kinase catalytic subunit type 3Add BLAST887

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei163Phosphothreonine; by AMPKBy similarity1
Modified residuei165Phosphoserine; by AMPKBy similarity1
Modified residuei244PhosphoserineBy similarity1
Modified residuei261PhosphoserineCombined sources1
Modified residuei282PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8NEB9.
MaxQBiQ8NEB9.
PaxDbiQ8NEB9.
PeptideAtlasiQ8NEB9.
PRIDEiQ8NEB9.

PTM databases

iPTMnetiQ8NEB9.
PhosphoSitePlusiQ8NEB9.

Expressioni

Tissue specificityi

Ubiquitously expressed, with a highest expression in skeletal muscle.1 Publication

Gene expression databases

BgeeiENSG00000078142.
CleanExiHS_PIK3C3.
ExpressionAtlasiQ8NEB9. baseline and differential.
GenevisibleiQ8NEB9. HS.

Organism-specific databases

HPAiHPA040718.

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: the PI3K complex I (PI3KC3-C1) containing ATG14, and the PI3K complex II (PI3KC3-C2) containing UVRAG. PI3KC3-C1 displays a V-shaped architecture with PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1 subcomplex. Both, PI3KC3-C1 and PI3KC3-C2, can associate with further regulatory subunits such as RUBCN, SH3GLB1/Bif-1 and AMBRA1 (PubMed:7628435, PubMed:19050071, PubMed:20643123, PubMed:19270696, PubMed:23878393, PubMed:25490155). PI3KC3-C1 probably associates with PIK3CB (By similarity). Interacts with RAB7A in the presence of PIK3R4 (PubMed:14617358). Interacts with AMBRA1 (By similarity). Interacts with BECN1P1/BECN2 (PubMed:23954414). Interacts with SLAMF1(PubMed:22493499). May be a component of a complex composed of RAB5A (in GDP-bound form), DYN2 and PIK3C3 (By similarity).By similarityCurated9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATG14Q6ZNE521EBI-1056470,EBI-2690371
BECN1Q1445724EBI-1056470,EBI-949378
NRBF2Q96F2411EBI-1056470,EBI-2362014
RUBCNQ926227EBI-1056470,EBI-2952709
UVRAGQ9P2Y516EBI-1056470,EBI-2952704

Protein-protein interaction databases

BioGridi111307. 35 interactors.
DIPiDIP-42272N.
IntActiQ8NEB9. 20 interactors.
MINTiMINT-1682773.
STRINGi9606.ENSP00000262039.

Chemistry databases

BindingDBiQ8NEB9.

Structurei

Secondary structure

1887
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi283 – 285Combined sources3
Helixi290 – 300Combined sources11
Beta strandi304 – 306Combined sources3
Helixi310 – 318Combined sources9
Helixi320 – 323Combined sources4
Helixi327 – 329Combined sources3
Helixi330 – 334Combined sources5
Helixi342 – 352Combined sources11
Helixi360 – 365Combined sources6
Helixi374 – 384Combined sources11
Helixi389 – 402Combined sources14
Helixi403 – 405Combined sources3
Helixi408 – 413Combined sources6
Helixi437 – 439Combined sources3
Helixi442 – 444Combined sources3
Turni445 – 447Combined sources3
Helixi475 – 485Combined sources11
Helixi487 – 502Combined sources16
Helixi504 – 509Combined sources6
Helixi511 – 529Combined sources19
Helixi533 – 561Combined sources29
Helixi566 – 578Combined sources13
Helixi580 – 583Combined sources4
Beta strandi591 – 593Combined sources3
Beta strandi596 – 604Combined sources9
Helixi606 – 608Combined sources3
Beta strandi613 – 616Combined sources4
Beta strandi619 – 625Combined sources7
Beta strandi630 – 639Combined sources10
Helixi642 – 660Combined sources19
Beta strandi672 – 683Combined sources12
Helixi690 – 697Combined sources8
Helixi700 – 707Combined sources8
Beta strandi711 – 713Combined sources3
Helixi714 – 716Combined sources3
Helixi719 – 738Combined sources20
Beta strandi748 – 751Combined sources4
Beta strandi757 – 759Combined sources3
Beta strandi770 – 773Combined sources4
Helixi781 – 787Combined sources7
Beta strandi790 – 792Combined sources3
Helixi793 – 811Combined sources19
Helixi813 – 821Combined sources9
Turni822 – 825Combined sources4
Helixi829 – 832Combined sources4
Helixi835 – 837Combined sources3
Helixi838 – 845Combined sources8
Turni846 – 849Combined sources4
Helixi852 – 872Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IHYX-ray2.80A/B/C/D/E282-879[»]
3LS8X-ray2.25A/B268-879[»]
4OYSX-ray2.90A282-879[»]
4PH4X-ray2.80B293-887[»]
4UWFX-ray2.99A282-879[»]
4UWGX-ray2.70A282-879[»]
4UWHX-ray1.93A282-879[»]
4UWKX-ray2.83A282-879[»]
4UWLX-ray2.80A282-879[»]
5ANLX-ray2.70A282-879[»]
ProteinModelPortaliQ8NEB9.
SMRiQ8NEB9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NEB9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 184C2 PI3K-typePROSITE-ProRule annotationAdd BLAST150
Domaini283 – 520PIK helicalPROSITE-ProRule annotationAdd BLAST238
Domaini631 – 885PI3K/PI4KPROSITE-ProRule annotationAdd BLAST255

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.PROSITE-ProRule annotation
Contains 1 C2 PI3K-type domain.PROSITE-ProRule annotation
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
Contains 1 PIK helical domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0906. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00760000119110.
HOGENOMiHOG000174003.
HOVERGENiHBG082145.
InParanoidiQ8NEB9.
KOiK00914.
OMAiWYYVIVE.
OrthoDBiEOG091G036A.
PhylomeDBiQ8NEB9.
TreeFamiTF102032.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
1.25.40.70. 2 hits.
2.60.40.150. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR002420. PI3K_C2_dom.
IPR008290. PI3K_Vps34.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
[Graphical view]
PANTHERiPTHR10048. PTHR10048. 2 hits.
PfamiPF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view]
PIRSFiPIRSF000587. PI3K_Vps34. 1 hit.
SMARTiSM00142. PI3K_C2. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8NEB9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEAEKFHYI YSCDLDINVQ LKIGSLEGKR EQKSYKAVLE DPMLKFSGLY
60 70 80 90 100
QETCSDLYVT CQVFAEGKPL ALPVRTSYKA FSTRWNWNEW LKLPVKYPDL
110 120 130 140 150
PRNAQVALTI WDVYGPGKAV PVGGTTVSLF GKYGMFRQGM HDLKVWPNVE
160 170 180 190 200
ADGSEPTKTP GRTSSTLSED QMSRLAKLTK AHRQGHMVKV DWLDRLTFRE
210 220 230 240 250
IEMINESEKR SSNFMYLMVE FRCVKCDDKE YGIVYYEKDG DESSPILTSF
260 270 280 290 300
ELVKVPDPQM SMENLVESKH HKLARSLRSG PSDHDLKPNA ATRDQLNIIV
310 320 330 340 350
SYPPTKQLTY EEQDLVWKFR YYLTNQEKAL TKFLKCVNWD LPQEAKQALE
360 370 380 390 400
LLGKWKPMDV EDSLELLSSH YTNPTVRRYA VARLRQADDE DLLMYLLQLV
410 420 430 440 450
QALKYENFDD IKNGLEPTKK DSQSSVSENV SNSGINSAEI DSSQIITSPL
460 470 480 490 500
PSVSSPPPAS KTKEVPDGEN LEQDLCTFLI SRACKNSTLA NYLYWYVIVE
510 520 530 540 550
CEDQDTQQRD PKTHEMYLNV MRRFSQALLK GDKSVRVMRS LLAAQQTFVD
560 570 580 590 600
RLVHLMKAVQ RESGNRKKKN ERLQALLGDN EKMNLSDVEL IPLPLEPQVK
610 620 630 640 650
IRGIIPETAT LFKSALMPAQ LFFKTEDGGK YPVIFKHGDD LRQDQLILQI
660 670 680 690 700
ISLMDKLLRK ENLDLKLTPY KVLATSTKHG FMQFIQSVPV AEVLDTEGSI
710 720 730 740 750
QNFFRKYAPS ENGPNGISAE VMDTYVKSCA GYCVITYILG VGDRHLDNLL
760 770 780 790 800
LTKTGKLFHI DFGYILGRDP KPLPPPMKLN KEMVEGMGGT QSEQYQEFRK
810 820 830 840 850
QCYTAFLHLR RYSNLILNLF SLMVDANIPD IALEPDKTVK KVQDKFRLDL
860 870 880
SDEEAVHYMQ SLIDESVHAL FAAVVEQIHK FAQYWRK
Length:887
Mass (Da):101,549
Last modified:October 1, 2002 - v1
Checksum:i1C03D97338E44976
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti36K → N in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti70L → S in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti136F → S in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti158K → N in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti208E → V in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti219 – 220VE → GG in CAA87094 (PubMed:7628435).Curated2
Sequence conflicti262M → L in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti272 – 274KLA → NLP in CAA87094 (PubMed:7628435).Curated3
Sequence conflicti289 – 292NAAT → YPSP in CAA87094 (PubMed:7628435).Curated4
Sequence conflicti297 – 298NI → KN in CAA87094 (PubMed:7628435).Curated2
Sequence conflicti305 – 308TKQL → SKPP in CAA87094 (PubMed:7628435).Curated4
Sequence conflicti318K → E in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti327E → D in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti333 – 338FLKCVN → ILTSVI in CAA87094 (PubMed:7628435).Curated6
Sequence conflicti344E → G in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti350E → A in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti356K → N in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti367L → I in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti397L → S in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti428E → G in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti484C → S in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti750L → V in CAA87094 (PubMed:7628435).Curated1
Sequence conflicti826A → P in CAA87094 (PubMed:7628435).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46973 mRNA. Translation: CAA87094.1.
BC033004 mRNA. Translation: AAH33004.1.
BC053651 mRNA. Translation: AAH53651.1.
CCDSiCCDS11920.1.
PIRiS57219.
RefSeqiNP_002638.2. NM_002647.3.
UniGeneiHs.464971.
Hs.656958.

Genome annotation databases

EnsembliENST00000262039; ENSP00000262039; ENSG00000078142.
GeneIDi5289.
KEGGihsa:5289.
UCSCiuc002lap.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46973 mRNA. Translation: CAA87094.1.
BC033004 mRNA. Translation: AAH33004.1.
BC053651 mRNA. Translation: AAH53651.1.
CCDSiCCDS11920.1.
PIRiS57219.
RefSeqiNP_002638.2. NM_002647.3.
UniGeneiHs.464971.
Hs.656958.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IHYX-ray2.80A/B/C/D/E282-879[»]
3LS8X-ray2.25A/B268-879[»]
4OYSX-ray2.90A282-879[»]
4PH4X-ray2.80B293-887[»]
4UWFX-ray2.99A282-879[»]
4UWGX-ray2.70A282-879[»]
4UWHX-ray1.93A282-879[»]
4UWKX-ray2.83A282-879[»]
4UWLX-ray2.80A282-879[»]
5ANLX-ray2.70A282-879[»]
ProteinModelPortaliQ8NEB9.
SMRiQ8NEB9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111307. 35 interactors.
DIPiDIP-42272N.
IntActiQ8NEB9. 20 interactors.
MINTiMINT-1682773.
STRINGi9606.ENSP00000262039.

Chemistry databases

BindingDBiQ8NEB9.
ChEMBLiCHEMBL1075165.
GuidetoPHARMACOLOGYi2152.
SwissLipidsiSLP:000000904.

PTM databases

iPTMnetiQ8NEB9.
PhosphoSitePlusiQ8NEB9.

Polymorphism and mutation databases

BioMutaiPIK3C3.
DMDMi74730233.

Proteomic databases

EPDiQ8NEB9.
MaxQBiQ8NEB9.
PaxDbiQ8NEB9.
PeptideAtlasiQ8NEB9.
PRIDEiQ8NEB9.

Protocols and materials databases

DNASUi5289.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262039; ENSP00000262039; ENSG00000078142.
GeneIDi5289.
KEGGihsa:5289.
UCSCiuc002lap.4. human.

Organism-specific databases

CTDi5289.
DisGeNETi5289.
GeneCardsiPIK3C3.
HGNCiHGNC:8974. PIK3C3.
HPAiHPA040718.
MIMi602609. gene.
neXtProtiNX_Q8NEB9.
OpenTargetsiENSG00000078142.
PharmGKBiPA33307.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0906. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00760000119110.
HOGENOMiHOG000174003.
HOVERGENiHBG082145.
InParanoidiQ8NEB9.
KOiK00914.
OMAiWYYVIVE.
OrthoDBiEOG091G036A.
PhylomeDBiQ8NEB9.
TreeFamiTF102032.

Enzyme and pathway databases

BioCyciMetaCyc:HS01275-MONOMER.
ZFISH:HS01275-MONOMER.
BRENDAi2.7.1.137. 2681.
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.
SIGNORiQ8NEB9.

Miscellaneous databases

ChiTaRSiPIK3C3. human.
EvolutionaryTraceiQ8NEB9.
GeneWikiiPIK3C3.
GenomeRNAii5289.
PROiQ8NEB9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000078142.
CleanExiHS_PIK3C3.
ExpressionAtlasiQ8NEB9. baseline and differential.
GenevisibleiQ8NEB9. HS.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
1.25.40.70. 2 hits.
2.60.40.150. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR002420. PI3K_C2_dom.
IPR008290. PI3K_Vps34.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
[Graphical view]
PANTHERiPTHR10048. PTHR10048. 2 hits.
PfamiPF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view]
PIRSFiPIRSF000587. PI3K_Vps34. 1 hit.
SMARTiSM00142. PI3K_C2. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPK3C3_HUMAN
AccessioniPrimary (citable) accession number: Q8NEB9
Secondary accession number(s): Q15134
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 142 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.