Phosphatidylinositol 3-kinase catalytic subunit type 3

Contribute

Send feedback

Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8NEB9 (PK3C3_HUMAN)

Last modified June 16, 2009. Version 59. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol 3-kinase catalytic subunit type 3
      Short name=PtdIns-3-kinase type 3
      Short name=PI3-kinase type 3
      Short name=PI3K type 3
    EC=2.7.1.137
Alternative name(s):
    Phosphoinositide-3-kinase class 3
    Phosphatidylinositol 3-kinase p100 subunit

Gene names

Name:

PIK3C3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	887 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Catalytic subunit of the PI3K complex. Involved in the transport of lysosomal enzyme precursors to lysosomes By similarity.
Catalytic activity	ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate.
Cofactor	Manganese. Ref.1
Subunit structure	Probably forms a complex with AMBRA1 and BECN1 By similarity. Heterodimer. This subunit, part of a complex composed of regulatory and catalytic subunits, associates with regulatory subunit PIK3R4.
Tissue specificity	Ubiquitously expressed, with a highest expression in skeletal muscle. Ref.1
Sequence similarities	Belongs to the PI3/PI4-kinase family. Contains 1 PI3K/PI4K domain.

Hide | Top

Ontologies

Keywords
Ligand	ATP-binding Manganese Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	phosphoinositide phosphorylation Inferred from electronic annotation. Source: InterPro phosphoinositide-mediated signaling Inferred from electronic annotation. Source: InterPro
Cellular component	phosphoinositide 3-kinase complex Inferred from electronic annotation. Source: InterPro
Molecular function	1-phosphatidylinositol-3-kinase activity Ref.1 Traceable author statement. Source: ProtInc ATP binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 887

887

Phosphatidylinositol 3-kinase catalytic subunit type 3

PRO_0000088802

Regions

Domain

631 – 885

255

PI3K/PI4K

Amino acid modifications

Modified residue

244

Phosphoserine Ref.3

Modified residue

448

Phosphoserine Ref.3

Modified residue

455

Phosphoserine Ref.3

Modified residue

525

Phosphoserine By similarity

Experimental info

Sequence conflict

K → N in CAA87094. Ref.1

Sequence conflict

L → S in CAA87094. Ref.1

Sequence conflict

136

F → S in CAA87094. Ref.1

Sequence conflict

158

K → N in CAA87094. Ref.1

Sequence conflict

208

E → V in CAA87094. Ref.1

Sequence conflict

219 – 220

VE → GG in CAA87094. Ref.1

Sequence conflict

262

M → L in CAA87094. Ref.1

Sequence conflict

272 – 274

KLA → NLP in CAA87094. Ref.1

Sequence conflict

289 – 292

NAAT → YPSP in CAA87094. Ref.1

Sequence conflict

297 – 298

NI → KN in CAA87094. Ref.1

Sequence conflict

305 – 308

TKQL → SKPP in CAA87094. Ref.1

Sequence conflict

318

K → E in CAA87094. Ref.1

Sequence conflict

327

E → D in CAA87094. Ref.1

Sequence conflict

333 – 338

FLKCVN → ILTSVI in CAA87094. Ref.1

Sequence conflict

344

E → G in CAA87094. Ref.1

Sequence conflict

350

E → A in CAA87094. Ref.1

Sequence conflict

356

K → N in CAA87094. Ref.1

Sequence conflict

367

L → I in CAA87094. Ref.1

Sequence conflict

397

L → S in CAA87094. Ref.1

Sequence conflict

428

E → G in CAA87094. Ref.1

Sequence conflict

484

C → S in CAA87094. Ref.1

Sequence conflict

750

L → V in CAA87094. Ref.1

Sequence conflict

826

A → P in CAA87094. Ref.1

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q8NEB9-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 1C03D97338E44976
Show »

FASTA

887

101,549

        10         20         30         40         50         60 
MGEAEKFHYI YSCDLDINVQ LKIGSLEGKR EQKSYKAVLE DPMLKFSGLY QETCSDLYVT 

        70         80         90        100        110        120 
CQVFAEGKPL ALPVRTSYKA FSTRWNWNEW LKLPVKYPDL PRNAQVALTI WDVYGPGKAV 

       130        140        150        160        170        180 
PVGGTTVSLF GKYGMFRQGM HDLKVWPNVE ADGSEPTKTP GRTSSTLSED QMSRLAKLTK 

       190        200        210        220        230        240 
AHRQGHMVKV DWLDRLTFRE IEMINESEKR SSNFMYLMVE FRCVKCDDKE YGIVYYEKDG 

       250        260        270        280        290        300 
DESSPILTSF ELVKVPDPQM SMENLVESKH HKLARSLRSG PSDHDLKPNA ATRDQLNIIV 

       310        320        330        340        350        360 
SYPPTKQLTY EEQDLVWKFR YYLTNQEKAL TKFLKCVNWD LPQEAKQALE LLGKWKPMDV 

       370        380        390        400        410        420 
EDSLELLSSH YTNPTVRRYA VARLRQADDE DLLMYLLQLV QALKYENFDD IKNGLEPTKK 

       430        440        450        460        470        480 
DSQSSVSENV SNSGINSAEI DSSQIITSPL PSVSSPPPAS KTKEVPDGEN LEQDLCTFLI 

       490        500        510        520        530        540 
SRACKNSTLA NYLYWYVIVE CEDQDTQQRD PKTHEMYLNV MRRFSQALLK GDKSVRVMRS 

       550        560        570        580        590        600 
LLAAQQTFVD RLVHLMKAVQ RESGNRKKKN ERLQALLGDN EKMNLSDVEL IPLPLEPQVK 

       610        620        630        640        650        660 
IRGIIPETAT LFKSALMPAQ LFFKTEDGGK YPVIFKHGDD LRQDQLILQI ISLMDKLLRK 

       670        680        690        700        710        720 
ENLDLKLTPY KVLATSTKHG FMQFIQSVPV AEVLDTEGSI QNFFRKYAPS ENGPNGISAE 

       730        740        750        760        770        780 
VMDTYVKSCA GYCVITYILG VGDRHLDNLL LTKTGKLFHI DFGYILGRDP KPLPPPMKLN 

       790        800        810        820        830        840 
KEMVEGMGGT QSEQYQEFRK QCYTAFLHLR RYSNLILNLF SLMVDANIPD IALEPDKTVK 

       850        860        870        880 
KVQDKFRLDL SDEEAVHYMQ SLIDESVHAL FAAVVEQIHK FAQYWRK

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7628435] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis and Uterus.
[3]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-448 AND SER-455, MASS SPECTROMETRY.
[4]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases
	Z46973 mRNA. Translation: CAA87094.1. BC033004 mRNA. Translation: AAH33004.1. BC053651 mRNA. Translation: AAH53651.1.
IPI	IPI00299755.
PIR	S57219.
RefSeq	NP_002638.2.
UniGene	Hs.464971
3D structure databases
HSSP	HSSP built from PDB template 1E8Y based on UniProtKB P48736.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8NEB9. 1 interaction.
PTM databases
PhosphoSite	Q8NEB9.
Proteomic databases
PeptideAtlas	Q8NEB9.
PRIDE	Q8NEB9.
Genome annotation databases
Ensembl	ENSG00000078142. Homo sapiens. [Contig view]
GeneID	5289.
KEGG	hsa:5289.
Organism-specific databases
GeneCards	GC18P037789.
H-InvDB	HIX0014414.
HGNC	HGNC:8974. PIK3C3.
MIM	602609. gene.
PharmGKB	PA33307.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q8NEB9.
HOVERGEN	Q8NEB9.
Enzyme and pathway databases
BRENDA	2.7.1.137. 247.
Reactome	REACT_6900. Signaling in Immune system.
Gene expression databases
ArrayExpress	Q8NEB9.
Bgee	Q8NEB9.
CleanEx	HS_PIK3C3.
GermOnline	ENSG00000078142. Homo sapiens.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR000403. PI3/4_kinase_cat. IPR018936. PI3/4_kinase_CS. IPR002420. PI3K_C2. IPR008290. PI3K_Vps34. IPR001263. PI3Ka. IPR015433. PI_Kinase. [Graphical view]
Gene3D	G3DSA:1.10.1070.11. PI3/4_kinase_cat. 1 hit. G3DSA:1.25.40.70. PI3Ka. 1 hit.
PANTHER	PTHR10048. PI_Kinase. 1 hit.
Pfam	PF00454. PI3_PI4_kinase. 1 hit. PF00792. PI3K_C2. 1 hit. PF00613. PI3Ka. 1 hit. [Graphical view]
PIRSF	PIRSF000587. PI3K_Vps34. 1 hit.
SMART	SM00239. C2. 1 hit. SM00142. PI3K_C2. 1 hit. SM00145. PI3Ka. 1 hit. SM00146. PI3Kc. 1 hit. [Graphical view]
PROSITE	PS00915. PI3_4_KINASE_1. 1 hit. PS00916. PI3_4_KINASE_2. 1 hit. PS50290. PI3_4_KINASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	20438.
SOURCE	Search...

Hide | Top

Entry information

Entry name

PK3C3_HUMAN

Accession

Primary (citable) accession number: Q8NEB9
Secondary accession number(s): Q15134

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents