Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P50520 (VPS34_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 3-kinase vps34

Short name=PI3-kinase vps34
Short name=PI3K vps34
Short name=PtdIns-3-kinase vps34
EC=2.7.1.137
Alternative name(s):
Vacuolar protein sorting-associated protein 34
Gene names
Name:vps34
ORF Names:SPAC458.05
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length801 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Phosphatidylinositol 3-kinase homolog required for vacuolar sorting and segregation.

Catalytic activity

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

Sequence similarities

Belongs to the PI3/PI4-kinase family.

Contains 1 C2 PI3K-type domain.

Contains 1 PI3K/PI4K domain.

Contains 1 PIK helical domain.

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein localization

Inferred from mutant phenotype PubMed 15189449. Source: PomBase

phosphatidylinositol metabolic process

Inferred from genetic interaction PubMed 15249580. Source: PomBase

phosphatidylinositol-3-phosphate biosynthetic process

Inferred from direct assay Ref.1. Source: PomBase

phosphatidylinositol-mediated signaling

Inferred from electronic annotation. Source: InterPro

positive regulation of ascospore formation

Inferred from mutant phenotype PubMed 12557273. Source: PomBase

protein localization to prospore membrane

Inferred from mutant phenotype PubMed 12557273. Source: PomBase

protein localization to vacuole

Inferred from mutant phenotype PubMed 12557273. Source: PomBase

vacuole organization

Inferred from mutant phenotype Ref.1. Source: PomBase

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 16823372. Source: PomBase

cytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

membrane

Inferred from mutant phenotype Ref.1. Source: PomBase

phosphatidylinositol 3-kinase complex

Inferred by curator. Source: PomBase

prospore membrane

Inferred from direct assay PubMed 12557273. Source: PomBase

vacuolar membrane

Inferred from direct assay PubMed 12557273. Source: PomBase

   Molecular_function1-phosphatidylinositol-3-kinase activity

Inferred from direct assay Ref.1. Source: PomBase

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 801801Phosphatidylinositol 3-kinase vps34
PRO_0000088817

Regions

Domain14 – 166153C2 PI3K-type
Domain257 – 439183PIK helical
Domain541 – 799259PI3K/PI4K

Experimental info

Sequence conflict1641K → Q in AAC49133. Ref.1
Sequence conflict2361L → I Ref.3
Sequence conflict6421S → T Ref.3

Sequences

Sequence LengthMass (Da)Tools
P50520 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: 520571E1475CC341

FASTA80192,135
        10         20         30         40         50         60 
MDRLVFSYCP SSKVTARFLV KFCFIEYQDS QEPCICTIQL FSGNESGSLM QKCFVSKIPN 

        70         80         90        100        110        120 
KSLLPTELSK ISTHEWLDFG VTVSELSLNA KFVVSAWKPS FNDEEVYEFV GCTTYRLFDE 

       130        140        150        160        170        180 
NNLLRQGLQK IPLQTSKEIK KYSPTSLELE QVKEINRLDG LLLKLQLGDV PSVNWLDDIS 

       190        200        210        220        230        240 
FGKIKDFRSK HMSLVTIPIL YLDFLQFSFP VVFQRSYYPK SENRVYYSSF DLELNLDSPA 

       250        260        270        280        290        300 
ELKHRRLVRS QRNGPLDKDL KPNSKIRKEL ESILSYPPSE ELSLEEKDLI WKFRFYLTRN 

       310        320        330        340        350        360 
KKAMTKFLKS VVWTDSSEVN QALSLLDSWT EIDIDDALEL LSPSFVHPKV RAYAVSRLET 

       370        380        390        400        410        420 
ASNEELLLYL LQLVQALRYD NPISSDERFQ PSPLALFLVN RAISSPSIGN DLYWYLVVEI 

       430        440        450        460        470        480 
EDEPVSKLFS SVMFLFQKEL SKSVEGRLIR ETLSAQAKFV EKLLRISKSV QSFRGTRLKK 

       490        500        510        520        530        540 
IEYLKVLLED HKYHLLDFHA LPLPLDPSVN IVGIIPDACT VFKSTMQPLR LLFKCQDGSK 

       550        560        570        580        590        600 
YPIIFKNGDD LRQDQLVIQI LTLMDKLLKK EKLDLHLKPY RILATGPTHG AVQFVPSKTL 

       610        620        630        640        650        660 
ATILAEYHGS VLAYLRENNP DDGLNSANYG IDPVAMDNYV RSCAGYCVIT YLLGVGDRHL 

       670        680        690        700        710        720 
DNLLITKDGH FFHADFGYIL GRDPKLFSPA MKLSKEMVEG MGGYNSPFYQ QFKSYCYTTF 

       730        740        750        760        770        780 
TALRKSSNLI LNLFSLMVDA NIPDIKFDKE KVVYKVKERF CLQMSESDAI KYFEQLINDS 

       790        800 
VSALFPQIID RMHNLAQYMR S 

« Hide

References

« Hide 'large scale' references
[1]"Schizosaccharomyces pombe Vps34p, a phosphatidylinositol-specific PI 3-kinase essential for normal cell growth and vacuole morphology."
Takegawa K., Dewald D.B., Emr S.E.
J. Cell Sci. 108:3745-3756(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Phosphatidylinositol-3 kinase in fission yeast: a possible role in stress responses."
Kimura K., Miyake S., Makuuchi M., Morita R., Usui T., Yoshida M., Horinouchi S., Fukui Y.
Biosci. Biotechnol. Biochem. 59:678-682(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 138-801.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U32583 mRNA. Translation: AAC49133.1.
CU329670 Genomic DNA. Translation: CAB93847.1.
PIRPC4002.
T52538.
RefSeqNP_594699.1. NM_001020127.2.

3D structure databases

ProteinModelPortalP50520.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279864. 3 interactions.
MINTMINT-4690623.
STRING4896.SPAC458.05-1.

Proteomic databases

MaxQBP50520.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC458.05.1; SPAC458.05.1:pep; SPAC458.05.
GeneID2543444.
KEGGspo:SPAC458.05.

Organism-specific databases

PomBaseSPAC458.05.

Phylogenomic databases

eggNOGCOG5032.
HOGENOMHOG000174003.
KOK00914.
OMAKISTHEW.
OrthoDBEOG7WHHK2.
PhylomeDBP50520.

Family and domain databases

Gene3D1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 1 hit.
InterProIPR016024. 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]
PANTHERPTHR10048. PTHR10048. 1 hit.
PfamPF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view]
PIRSFPIRSF000587. PI3K_Vps34. 1 hit.
SMARTSM00142. PI3K_C2. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00915. 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]
ProtoNetSearch...

Other

NextBio20804457.
PROP50520.

Entry information

Entry nameVPS34_SCHPO
AccessionPrimary (citable) accession number: P50520
Secondary accession number(s): Q9P3W3, Q9URD2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 14, 2001
Last modified: June 11, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names