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Showing Protein Phosphatidylinositol 3-kinase catalytic subunit type 3 (HMDBP03992)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 383 metabolites
Identification
HMDB Protein ID HMDBP03992
Secondary Accession Numbers
  • 9581
Name Phosphatidylinositol 3-kinase catalytic subunit type 3
Synonyms
  1. PI3-kinase type 3
  2. PI3K type 3
  3. Phosphatidylinositol 3-kinase p100 subunit
  4. Phosphoinositide-3-kinase class 3
  5. PtdIns-3-kinase type 3
  6. hVps34
Gene Name PIK3C3
Protein Type Unknown
Biological Properties
General Function Involved in binding
Specific Function Catalytic subunit of the PI3K complex. Involved in the transport of lysosomal enzyme precursors to lysosomes
Pathways
  • Inositol phosphate metabolism
  • Joubert syndrome
  • Phosphatidylinositol Phosphate Metabolism
Reactions Not Available
GO Classification
Component
macromolecular complex
protein complex
phosphoinositide 3-kinase complex
Function
binding
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
phosphotransferase activity, alcohol group as acceptor
inositol or phosphatidylinositol kinase activity
lipid kinase activity
phosphoinositide 3-kinase activity
1-phosphatidylinositol-3-kinase activity
Process
metabolic process
biological regulation
regulation of biological process
regulation of cellular process
signal transduction
intracellular signal transduction
organophosphate metabolic process
phospholipid metabolic process
second-messenger-mediated signaling
phosphoinositide-mediated signaling
glycerophospholipid metabolic process
phosphoinositide metabolic process
phosphoinositide phosphorylation
Cellular Location Not Available
Gene Properties
Chromosome Location Chromosome:1
Locus 18q12.3
SNPs PIK3C3
Gene Sequence 
>2664 bp
ATGGGGGAAGCAGAGAAGTTTCACTACATCTATAGTTGTGACCTGGATATCAACGTCCAG
CTTAAGATAGGAAGCTTGGAAGGGAAGAGAGAACAAAAGAGTTATAACGCTGTCCTGGAA
GACCCAATGTTGAAGTTCTCAGGACTATATCAAGAGACATGCTCTGATCTTTATGTTACT
TGTCAAGTTTTTGCAGAAGGGAAGCCTTCGGCCTTGCCAGTGAGAACATCCTACAAAGCA
TTTAGTACAAGATGGAACTGGAATGAATGGCTGAAACTACCAGTAAAATACCCTGACCTG
CCCAGGAATGCCCAAGTGGCCCTCACCATATGGGATGTGTATGGTCCCGGAAAAGCAGTG
CCTGTAGGAGGAACAACGGTTTCGCTCTTTGGAAAATACGGCATGTCTCGCCAAGGGATG
CATGACTTGAAAGTCTGGCCTAATGTAGAAGCAGATGGATCAGAACCCACAAATACTCCT
GGCAGAACAAGTAGCACTCTCTCAGAAGATCAGATGAGCCGTCTTGCCAAGCTCACCAAA
GCTCATCGACAAGGACACATGGTGAAAGTAGATTGGCTGGATAGATTGACATTTAGAGAA
ATAGAAATGATAAATGAGAGTGTGAAACGAAGTTCTAATTTCATGTACCTGATGGGTGGA
TTTCGATGTGTCAAGTGTGATGATAAGGAATATGGTATTGTTTATTATGAAAAGGACGGT
GATGAATCATCTCCAATTTTAACAAGTTTTGAATTAGTGAAAGTTCCTGACCCCCAGATG
TCCCTGGAGAATTTAGTTGAGAGCAAACACCACAACCTTCCCCGGAGTTTAAGAAGTGGA
CCTTCTGACCACGATCTGAAACCCTATCCTTCCCCGAGAGATCAGTTAAAAAATATTGTG
AGTTATCCTCCATCCAAGCCACCCACATATGAAGAACAAGATCTTGTTTGGGAGTTTAGA
TATTATCTTACGAATCAAGATAAAGCCTTGACCAAAATCCTGACATCTGTTATTTGGGAT
CTACCTCAGGGGGCCAAACAGGCCTTGGCACTTCTGGGGAAATGGAACCCGATGGATGTA
GAGGACTCCTTGGAGCTGATATCCTCTCATTACACCAACCCAACTGTGAGGCGTTATGCT
GTTGCCCGGTTGCGACAGGCCGATGATGAGGATTTGTTGATGTACCTATCACAATTGGTC
CAGGCTCTCAAATATGAAAATTTTGATGATATAAAGAATGGATTGGAACCTACCAAGAAG
GATAGTCAGAGTTCAGTGTCAGGAAATGTGTCAAATTCTGGAATAAATTCTGCAGAAATA
GATAGCTCCCAAATTATAACCAGCCCCCTTCCTTCAGTCTCTTCACCTCCTCCTGCATCA
AAAACAAAAGAAGTTCCAGATGGCGAAAATCTGGAACAAGATCTCTGTACCTTCTTGATA
TCGAGAGCCTCCAAAAACTCAACACTGGCTAATTATTTATACTGGTATGTGATAGTGGAA
TGTGAAGATCAAGATACTCAGCAGAGAGATCCAAAGACCCATGAGATGTACTTGAACGTA
ATGAGAAGATTCAGCCAAGCATTGTTGAAGGGTGATAAGTCTGTCAGAGTTATGCGTTCT
TTGCTGGCTGCACAACAGACATTTGTAGATCGGTTGGTGCATCTAATGAAGGCAGTACAA
CGCGAAAGTGGAAATCGTAAGAAAAAGAATGAGAGACTACAGGCATTGCTTGGAGATAAT
GAAAAGATGAATTTGTCAGATGTGGAACTTATCCCGTTGCCTTTAGAACCCCAAGTGAAA
ATTAGAGGAATAATTCCGGAAACAGCTACACTGTTTAAAAGTGCCCTTATGCCTGCACAG
TTGTTTTTTAAGACGGAAGATGGAGGCAAATATCCAGTTATATTTAAGCATGGAGATGAT
TTACGTCAAGATCAACTTATTCTTCAAATCATTTCACTCATGGACAAGCTGTTACGGAAA
GAAAATCTGGACTTGAAATTGACACCTTATAAGGTGTTAGCCACCAGTACAAAACATGGC
TTCATGCAGTTTATCCAGTCAGTTCCTGTGGCTGAAGTTCTTGATACAGAGGGAAGCATT
CAGAACTTTTTTAGAAAATATGCACCAAGTGAGAATGGGCCAAATGGGATTAGTGCTGAG
GTCATGGACACTTACGTTAAAAGCTGTGCTGGATATTGCGTGATCACCTATATACTTGGA
GTTGGAGACAGGCACCTGGATAACCTTGTGCTAACAAAAACAGGCAAACTCTTCCACATA
GACTTTGGATATATTTTGGGTCGGGATCCAAAGCCTCTTCCTCCACCAATGAAGCTGAAT
AAAGAAATGGTAGAAGGAATGGGGGGCACACAGAGTGAGCAGTACCAAGAGTTCCGTAAA
CAGTGTTACACGGCTTTCCTCCACCTGCGGAGGTATTCTAATCTGATTTTGAACTTGTTT
TCCTTGATGGTTGATCCAAACATTCCAGATATTGCACTTGAACCAGATAAAACTGTGAAA
AAGGTTCAGGATAAATTCCGCTTAGACCTGTCGGATGAAGAGGCTGTGCATTACATGCAG
AGTCTGATTGATGAGAGTGTCCATGCTCTTTTTGCTGCAGTGGTGGAACAGATTCACAAG
TTTGCCCAGTACTGGAGAAAATGA
Protein Properties
Number of Residues 887
Molecular Weight 101548.6
Theoretical pI 6.79
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Phosphatidylinositol 3-kinase catalytic subunit type 3
MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVT
CQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAV
PVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTK
AHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDG
DESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIV
SYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDV
EDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKK
DSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLI
SRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRS
LLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVK
IRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRK
ENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAE
VMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLN
KEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVK
KVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK
GenBank ID Protein 987948
UniProtKB/Swiss-Prot ID Q8NEB9
UniProtKB/Swiss-Prot Entry Name PK3C3_HUMAN
PDB IDs Not Available
GenBank Gene ID Z46973
GeneCard ID PIK3C3
GenAtlas ID PIK3C3
HGNC ID HGNC:8974
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  3. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  5. Volinia S, Dhand R, Vanhaesebroeck B, MacDougall LK, Stein R, Zvelebil MJ, Domin J, Panaretou C, Waterfield MD: A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system. EMBO J. 1995 Jul 17;14(14):3339-48. [PubMed:7628435 ]
  6. Sun Q, Fan W, Chen K, Ding X, Chen S, Zhong Q: Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase. Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19211-6. doi: 10.1073/pnas.0810452105. Epub 2008 Dec 2. [PubMed:19050071 ]
  7. 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: Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages. Nat Cell Biol. 2009 Apr;11(4):385-96. doi: 10.1038/ncb1846. Epub 2009 Mar 8. [PubMed:19270696 ]