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Q8NEB9

- PK3C3_HUMAN

UniProt

Q8NEB9 - PK3C3_HUMAN

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Protein

Phosphatidylinositol 3-kinase catalytic subunit type 3

Gene

PIK3C3

Organism
Homo sapiens (Human)
Status
Reviewed - 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 which plays a key role in initiation and maturation of autophagosomes. Involved in the transport of lysosomal enzyme precursors to lysosomes. Required for the abcission step in cytokinesis. Required for transport from early to late endosomes.3 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. 1-phosphatidylinositol-3-kinase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. protein kinase activity Source: Ensembl

GO - Biological processi

  1. autophagic vacuole assembly Source: Ensembl
  2. cytokinesis Source: UniProtKB
  3. early endosome to late endosome transport Source: UniProtKB
  4. endosome organization Source: Ensembl
  5. innate immune response Source: Reactome
  6. insulin receptor signaling pathway Source: Reactome
  7. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  8. phosphatidylinositol biosynthetic process Source: Reactome
  9. phosphatidylinositol-mediated signaling Source: Ensembl
  10. phospholipid metabolic process Source: Reactome
  11. protein processing Source: Ensembl
  12. regulation of protein secretion Source: Ensembl
  13. response to leucine Source: Ensembl
  14. small molecule metabolic process Source: Reactome
  15. toll-like receptor 9 signaling pathway Source: Reactome
  16. toll-like receptor 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.
ReactomeiREACT_120756. Synthesis of PIPs at the early endosome membrane.
REACT_120836. Synthesis of PIPs at the Golgi membrane.
REACT_120918. Synthesis of PIPs at the late endosome membrane.
REACT_9047. Toll Like Receptor 9 (TLR9) Cascade.
REACT_976. PI3K Cascade.

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
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:8974. PIK3C3.

Subcellular locationi

Midbody. Late endosome
Note: Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme.By similarity

GO - Cellular componenti

  1. axoneme Source: UniProtKB
  2. cytosol Source: Reactome
  3. late endosome Source: UniProtKB
  4. membrane Source: UniProtKB
  5. midbody Source: UniProtKB
  6. phagocytic vesicle Source: Ensembl
  7. phosphatidylinositol 3-kinase complex Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Endosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33307.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 887887Phosphatidylinositol 3-kinase catalytic subunit type 3PRO_0000088802Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei261 – 2611Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8NEB9.
PaxDbiQ8NEB9.
PeptideAtlasiQ8NEB9.
PRIDEiQ8NEB9.

PTM databases

PhosphoSiteiQ8NEB9.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ8NEB9.
CleanExiHS_PIK3C3.
ExpressionAtlasiQ8NEB9. baseline and differential.
GenevestigatoriQ8NEB9.

Organism-specific databases

HPAiHPA040718.

Interactioni

Subunit structurei

Heterodimer. This subunit, part of a complex composed of regulatory and catalytic subunits, associates with regulatory subunit PIK3R4. Forms a complex with BECN1, PIK3R4 and either UVRAG and KIAA0226/Rubicon, or with ATG14. In this complex, presence of UVRAG and ATG14 are mutually exclusive. Part of a complex composed of PIK3R4 and PIK3CB (By similarity). Interacts with RAB7A in the presence of PIK3R4. Interacts with BECN1P1/BECN2.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BECN1Q1445714EBI-1056470,EBI-949378

Protein-protein interaction databases

BioGridi111307. 33 interactions.
DIPiDIP-42272N.
IntActiQ8NEB9. 12 interactions.
MINTiMINT-1682773.
STRINGi9606.ENSP00000262039.

Structurei

Secondary structure

1
887
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi283 – 2853Combined sources
Helixi290 – 30112Combined sources
Helixi310 – 3189Combined sources
Helixi320 – 3234Combined sources
Helixi327 – 3293Combined sources
Helixi330 – 3345Combined sources
Helixi342 – 35413Combined sources
Helixi360 – 3634Combined sources
Helixi364 – 3674Combined sources
Helixi374 – 38411Combined sources
Helixi389 – 3946Combined sources
Helixi396 – 4027Combined sources
Helixi403 – 4053Combined sources
Helixi408 – 4136Combined sources
Helixi442 – 4443Combined sources
Helixi475 – 48410Combined sources
Helixi487 – 50216Combined sources
Helixi504 – 5096Combined sources
Helixi511 – 53020Combined sources
Helixi533 – 56129Combined sources
Helixi566 – 57813Combined sources
Helixi580 – 5834Combined sources
Beta strandi589 – 5935Combined sources
Beta strandi596 – 6049Combined sources
Helixi606 – 6083Combined sources
Beta strandi619 – 6257Combined sources
Beta strandi630 – 63910Combined sources
Helixi642 – 66019Combined sources
Beta strandi672 – 68312Combined sources
Helixi690 – 6967Combined sources
Helixi700 – 7078Combined sources
Helixi714 – 7163Combined sources
Helixi719 – 73921Combined sources
Beta strandi748 – 7514Combined sources
Beta strandi757 – 7593Combined sources
Beta strandi770 – 7734Combined sources
Helixi781 – 7866Combined sources
Helixi793 – 81119Combined sources
Helixi813 – 8219Combined sources
Turni822 – 8254Combined sources
Helixi829 – 8324Combined sources
Helixi835 – 8373Combined sources
Helixi838 – 8458Combined sources
Turni846 – 8494Combined sources
Helixi852 – 87019Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IHYX-ray2.80A/B/C/D/E282-879[»]
3LS8X-ray2.25A/B268-879[»]
ProteinModelPortaliQ8NEB9.
SMRiQ8NEB9. Positions 12-881.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NEB9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 184150C2 PI3K-typePROSITE-ProRule annotationAdd
BLAST
Domaini283 – 520238PIK helicalPROSITE-ProRule annotationAdd
BLAST
Domaini631 – 885255PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG5032.
GeneTreeiENSGT00760000119110.
HOGENOMiHOG000174003.
HOVERGENiHBG082145.
InParanoidiQ8NEB9.
KOiK00914.
OMAiYLMVEFP.
OrthoDBiEOG7PP55Z.
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. 1 hit.
PfamiPF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view]
PIRSFiPIRSF000587. PI3K_Vps34. 1 hit.
SMARTiSM00239. C2. 1 hit.
SM00142. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361K → N in CAA87094. (PubMed:7628435)Curated
Sequence conflicti70 – 701L → S in CAA87094. (PubMed:7628435)Curated
Sequence conflicti136 – 1361F → S in CAA87094. (PubMed:7628435)Curated
Sequence conflicti158 – 1581K → N in CAA87094. (PubMed:7628435)Curated
Sequence conflicti208 – 2081E → V in CAA87094. (PubMed:7628435)Curated
Sequence conflicti219 – 2202VE → GG in CAA87094. (PubMed:7628435)Curated
Sequence conflicti262 – 2621M → L in CAA87094. (PubMed:7628435)Curated
Sequence conflicti272 – 2743KLA → NLP in CAA87094. (PubMed:7628435)Curated
Sequence conflicti289 – 2924NAAT → YPSP in CAA87094. (PubMed:7628435)Curated
Sequence conflicti297 – 2982NI → KN in CAA87094. (PubMed:7628435)Curated
Sequence conflicti305 – 3084TKQL → SKPP in CAA87094. (PubMed:7628435)Curated
Sequence conflicti318 – 3181K → E in CAA87094. (PubMed:7628435)Curated
Sequence conflicti327 – 3271E → D in CAA87094. (PubMed:7628435)Curated
Sequence conflicti333 – 3386FLKCVN → ILTSVI in CAA87094. (PubMed:7628435)Curated
Sequence conflicti344 – 3441E → G in CAA87094. (PubMed:7628435)Curated
Sequence conflicti350 – 3501E → A in CAA87094. (PubMed:7628435)Curated
Sequence conflicti356 – 3561K → N in CAA87094. (PubMed:7628435)Curated
Sequence conflicti367 – 3671L → I in CAA87094. (PubMed:7628435)Curated
Sequence conflicti397 – 3971L → S in CAA87094. (PubMed:7628435)Curated
Sequence conflicti428 – 4281E → G in CAA87094. (PubMed:7628435)Curated
Sequence conflicti484 – 4841C → S in CAA87094. (PubMed:7628435)Curated
Sequence conflicti750 – 7501L → V in CAA87094. (PubMed:7628435)Curated
Sequence conflicti826 – 8261A → P in CAA87094. (PubMed:7628435)Curated

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_002647.2.
UniGeneiHs.464971.

Genome annotation databases

EnsembliENST00000262039; ENSP00000262039; ENSG00000078142.
GeneIDi5289.
KEGGihsa:5289.
UCSCiuc002lap.3. human.

Polymorphism databases

DMDMi74730233.

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 .
CCDSi CCDS11920.1.
PIRi S57219.
RefSeqi NP_002638.2. NM_002647.2.
UniGenei Hs.464971.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IHY X-ray 2.80 A/B/C/D/E 282-879 [» ]
3LS8 X-ray 2.25 A/B 268-879 [» ]
ProteinModelPortali Q8NEB9.
SMRi Q8NEB9. Positions 12-881.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111307. 33 interactions.
DIPi DIP-42272N.
IntActi Q8NEB9. 12 interactions.
MINTi MINT-1682773.
STRINGi 9606.ENSP00000262039.

Chemistry

BindingDBi Q8NEB9.
ChEMBLi CHEMBL1075165.

PTM databases

PhosphoSitei Q8NEB9.

Polymorphism databases

DMDMi 74730233.

Proteomic databases

MaxQBi Q8NEB9.
PaxDbi Q8NEB9.
PeptideAtlasi Q8NEB9.
PRIDEi Q8NEB9.

Protocols and materials databases

DNASUi 5289.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262039 ; ENSP00000262039 ; ENSG00000078142 .
GeneIDi 5289.
KEGGi hsa:5289.
UCSCi uc002lap.3. human.

Organism-specific databases

CTDi 5289.
GeneCardsi GC18P039535.
HGNCi HGNC:8974. PIK3C3.
HPAi HPA040718.
MIMi 602609. gene.
neXtProti NX_Q8NEB9.
PharmGKBi PA33307.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5032.
GeneTreei ENSGT00760000119110.
HOGENOMi HOG000174003.
HOVERGENi HBG082145.
InParanoidi Q8NEB9.
KOi K00914.
OMAi YLMVEFP.
OrthoDBi EOG7PP55Z.
PhylomeDBi Q8NEB9.
TreeFami TF102032.

Enzyme and pathway databases

BioCyci MetaCyc:HS01275-MONOMER.
Reactomei REACT_120756. Synthesis of PIPs at the early endosome membrane.
REACT_120836. Synthesis of PIPs at the Golgi membrane.
REACT_120918. Synthesis of PIPs at the late endosome membrane.
REACT_9047. Toll Like Receptor 9 (TLR9) Cascade.
REACT_976. PI3K Cascade.

Miscellaneous databases

ChiTaRSi PIK3C3. human.
EvolutionaryTracei Q8NEB9.
GeneWikii PIK3C3.
GenomeRNAii 5289.
NextBioi 20438.
PROi Q8NEB9.
SOURCEi Search...

Gene expression databases

Bgeei Q8NEB9.
CleanExi HS_PIK3C3.
ExpressionAtlasi Q8NEB9. baseline and differential.
Genevestigatori Q8NEB9.

Family and domain databases

Gene3Di 1.10.1070.11. 1 hit.
1.25.40.70. 2 hits.
2.60.40.150. 1 hit.
InterProi IPR016024. 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 ]
PANTHERi PTHR10048. PTHR10048. 1 hit.
Pfami PF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view ]
PIRSFi PIRSF000587. PI3K_Vps34. 1 hit.
SMARTi SM00239. C2. 1 hit.
SM00142. PI3K_C2. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 2 hits.
SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00915. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system."
    Volinia S., Dhand R., Vanhaesebroeck B., MacDougall L.K., Zvelebil M.J., Domin J., Panaretou C., Waterfield M.D.
    EMBO J. 14:3339-3348(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, SUBUNIT, TISSUE SPECIFICITY, INTERACTION WITH PIK3R4.
  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].
    Tissue: Testis and Uterus.
  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: FUNCTION, INTERACTION WITH RAB7A AND PIK3R4, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase."
    Sun Q., Fan W., Chen K., Ding X., Chen S., Zhong Q.
    Proc. Natl. Acad. Sci. U.S.A. 105:19211-19216(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BECN1 AND ATG14.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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; KIAA0226; ATG14; PIK3R4 AND UVRAG.
  8. "PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of FYVE-CENT to the midbody."
    Sagona A.P., Nezis I.P., Pedersen N.M., Liestol K., Poulton J., Rusten T.E., Skotheim R.I., Raiborg C., Stenmark H.
    Nat. Cell Biol. 12:362-371(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Beclin 2 functions in autophagy, degradation of G protein-coupled receptors, and metabolism."
    He C., Wei Y., Sun K., Li B., Dong X., Zou Z., Liu Y., Kinch L.N., Khan S., Sinha S., Xavier R.J., Grishin N.V., Xiao G., Eskelinen E.L., Scherer P.E., Whistler J.L., Levine B.
    Cell 154:1085-1099(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BECN1P1/BECN2.

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 26, 2014
This is version 120 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

External Data

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