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Protein

1-phosphatidylinositol 3-phosphate 5-kinase fab1

Gene

fab1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (By similarity). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. The product of the reaction it catalyzes functions as an important regulator of vacuole homeostasis perhaps by controlling membrane flux to and/or from the vacuole (By similarity). Required for survival under conditions of nitrogen starvation. May have a role in the secretion of pheromone peptides.By similarity1 Publication

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri60 – 11960FYVE-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cellular response to nitrogen starvation Source: PomBase
  • pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: PomBase
  • phosphatidylinositol metabolic process Source: PomBase
  • phosphatidylinositol phosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-1660514. Synthesis of PIPs at the Golgi membrane.
R-SPO-1660516. Synthesis of PIPs at the early endosome membrane.
R-SPO-1660517. Synthesis of PIPs at the late endosome membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 3-phosphate 5-kinase fab1 (EC:2.7.1.150)
Short name:
Phosphatidylinositol 3-phosphate 5-kinase
Alternative name(s):
Diphosphoinositide kinase
Type III PIP kinase
Short name:
PIPkin-III
Gene namesi
Name:fab1
Synonyms:ste12
ORF Names:SPBC3E7.01, SPBC6B1.11c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC3E7.01.
PomBaseiSPBC3E7.01. fab1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 193219321-phosphatidylinositol 3-phosphate 5-kinase fab1PRO_0000185450Add
BLAST

Proteomic databases

MaxQBiO59722.

Interactioni

Subunit structurei

Component of the PI(3,5)P2 regulatory complex, at least composed of fab1, fig4/SPAC1093.03 and vac14/SPBC25H2.03. Vac14 nucleates the assembly of the complex and serves as a scaffold.By similarity

Protein-protein interaction databases

BioGridi277669. 6 interactions.

Structurei

3D structure databases

ProteinModelPortaliO59722.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1590 – 1916327PIPKPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation
Contains 1 PIPK domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri60 – 11960FYVE-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

InParanoidiO59722.
KOiK00921.
OMAiCETHGNA.
OrthoDBiEOG776SZ7.
PhylomeDBiO59722.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.30.800.10. 1 hit.
3.30.810.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
PF01363. FYVE. 1 hit.
PF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00330. PIPKc. 1 hit.
[Graphical view]
SUPFAMiSSF52029. SSF52029. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51455. PIPK. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O59722-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEVETPTAA SPTFPVETSH RLDTLHTSST EQIIKDSENV VHTTLKLPTS
60 70 80 90 100
TLSREFWMKD ERTNNCSLCE TEFTLFRRKH HCRICGKIIC KYCLKEAPGF
110 120 130 140 150
IFRLQGSIKV CRPCASILVN NYSRSQLFNH SLNESKNRDL TEQHPFVTLD
160 170 180 190 200
ELNSNDQVLS SFGDLSSTFE MPNNIHPPEV APMIAIPSSR SNYDSPGWAH
210 220 230 240 250
HSIFLDWSKR NLDSNVINVE DSESGKYNAL TITNSYDAGP SSVSTDYRPV
260 270 280 290 300
NFGKVPSYSK LRKNKAFSSA KVSDMYLSAD ERNRLEDFSK GDRGLSFVNL
310 320 330 340 350
SPNIKATSYD RLSTVINEPF ISRSSSLTDE RGLADSGNSY HHFSDSDDES
360 370 380 390 400
LFNDGLGLSF HANSAIIKQR QQNVASIQRY GNESYLSNFL KAFLPKTVCD
410 420 430 440 450
YLFPSSTIPD GLPALIENFN ARVDKVNHPG GTEEPLPYQG KSRASSVVTS
460 470 480 490 500
SKSTCILPPW ILFSDSFNQL VCTFLGKLLF QMLNDEGVDS PMQWVLCLPK
510 520 530 540 550
ILLKMALDLG PDIRSGDDID VRSYVKIKKI PGGSIQDCFL VNGVLFSKKA
560 570 580 590 600
SSKSMDRSLR RPRIALLTFS LDYACDEQRI LSLDLIISQQ EEYIINLVNR
610 620 630 640 650
ICMLKPNLVF AQGQIPSIAL KYFEEHGVIA FHGLKESVLY DIARCCRADI
660 670 680 690 700
ISSIDKLSLC PRLGTCGRFQ LRTYVVDENK GLRKTFAILD RCSERLGCTI
710 720 730 740 750
VLRGADYNQL SKVKKIVELV VLIAYHIKLE CALLRDKFVN MPELFETTYQ
760 770 780 790 800
SLSRKSLPSF ASTAADKEKS QNHEKKSLNS DNQSLRPLEN ENQSVSSTQG
810 820 830 840 850
SNSPLELINN LPASDDYSSI TKALKTRFLT FSPFLSKPLP RLLNQVNYYQ
860 870 880 890 900
FIRNKLLKDV KLHPYSPTGS FVMKQSENDN VEESYEESYK FFCIDERYHF
910 920 930 940 950
LEKQWTLYYS HSKLMFSPFS SQRIILLYSI INKETSVPCI GPERCLLEFY
960 970 980 990 1000
RETDCTLGQY IEDSCLNTNV SCGGEYCKTN DMLWHYRSYV HGNSRISVFL
1010 1020 1030 1040 1050
ESFSCPVPGL EEKIIMWSYC KFCKKNTHIT VMSEETWKYS FGKYLEFMFY
1060 1070 1080 1090 1100
NSQIRDRFEF CDHSVMAQHV HYFGYCNMAL RFQRDLIEIF ELFVPSVTLR
1110 1120 1130 1140 1150
NNPSYIKELK EKEYKRLKGV IEKCLSSVAS RINQIKCDWV TDPEKFESCT
1160 1170 1180 1190 1200
SEISKFRTLL SSDYTELYSE FDSIYLNSST SDYLSLNSIL RVLQGKMVKW
1210 1220 1230 1240 1250
EQRFLDYQRL YLPSYKELSK IAAAQIKKVF LERPLSQTPL DLPETLENTQ
1260 1270 1280 1290 1300
IDIYPSFKTE STDDQLEKVT QTNVASNKRV APYADSMANV GSPESDCFSV
1310 1320 1330 1340 1350
ATSSDIPKAN IDFTNDISTQ NTFPASPVSN SGFSRQTYPN ISQRQGVNML
1360 1370 1380 1390 1400
SHKRKSASTS DRRFVNASST SGMNMPISSS ISAKISSIQN STKYSPRKPI
1410 1420 1430 1440 1450
PAKDVRVSSL VRRFEELSLQ LQEKQKRDEE LIKARRKRAL PVVPSKPVVE
1460 1470 1480 1490 1500
VFNDLNEAFD DENSEDENGI NDTKENRATE SNFSGVDSMS KERENVSSNE
1510 1520 1530 1540 1550
DNSPEAFEDI FGILFKNESG LEEQQNLEPS SQMDKEGSKL PTSGPLADKT
1560 1570 1580 1590 1600
SVYRILSAFW NEWNSLNPPP FEFPLQPTEH MFSDSNVIIR EDEPSSLISF
1610 1620 1630 1640 1650
TLSSPDYLSK MVEIEDSMDE ALTNQGLQGS TQFKIENLML KPTGTHLKYQ
1660 1670 1680 1690 1700
FEEGSARLSC KVFFAEQFSA LRRACGCEET FVTSLARCSL WESSGGKSGS
1710 1720 1730 1740 1750
AFLKTFDKKY ILKVLSRLES DSLLNFAPAY FDYISKVFFH ELPTALTKIF
1760 1770 1780 1790 1800
GFYRVDIRNP TTGTICKTDI MIMENVFYDE CPSRIFDLKG SMRNRHVEST
1810 1820 1830 1840 1850
GKVDEVLLDE NLVELIYESP IFVSEQLKSL LHSCLWNDTL FLSKLNIMDY
1860 1870 1880 1890 1900
SLIVGIDYTK KELYVGIIDF IRTYTWDKKL ESWVKEKGLV GRGPEPTIVT
1910 1920 1930
PKQYKNRFRK AMDCYILASQ DFETGEGFKF CE
Length:1,932
Mass (Da):220,135
Last modified:May 16, 2003 - v2
Checksum:iB9826516D4504229
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA17054.1.
PIRiT40375.
T40652.
RefSeqiNP_596090.2. NM_001022005.3.

Genome annotation databases

EnsemblFungiiSPBC3E7.01.1; SPBC3E7.01.1:pep; SPBC3E7.01.
GeneIDi2541154.
KEGGispo:SPBC3E7.01.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA17054.1.
PIRiT40375.
T40652.
RefSeqiNP_596090.2. NM_001022005.3.

3D structure databases

ProteinModelPortaliO59722.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277669. 6 interactions.

Proteomic databases

MaxQBiO59722.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC3E7.01.1; SPBC3E7.01.1:pep; SPBC3E7.01.
GeneIDi2541154.
KEGGispo:SPBC3E7.01.

Organism-specific databases

EuPathDBiFungiDB:SPBC3E7.01.
PomBaseiSPBC3E7.01. fab1.

Phylogenomic databases

InParanoidiO59722.
KOiK00921.
OMAiCETHGNA.
OrthoDBiEOG776SZ7.
PhylomeDBiO59722.

Enzyme and pathway databases

ReactomeiR-SPO-1660514. Synthesis of PIPs at the Golgi membrane.
R-SPO-1660516. Synthesis of PIPs at the early endosome membrane.
R-SPO-1660517. Synthesis of PIPs at the late endosome membrane.

Miscellaneous databases

NextBioi20802267.
PROiO59722.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.30.800.10. 1 hit.
3.30.810.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
PF01363. FYVE. 1 hit.
PF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00330. PIPKc. 1 hit.
[Graphical view]
SUPFAMiSSF52029. SSF52029. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51455. PIPK. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Phosphatidylinositol 3-phosphate 5-kinase is required for the cellular response to nutritional starvation and mating pheromone signals in Schizosaccharomyces pombe."
    Morishita M., Morimoto F., Kitamura K., Koga T., Fukui Y., Maekawa H., Yamashita I., Shimoda C.
    Genes Cells 7:199-215(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  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.
    , 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.

Entry informationi

Entry nameiFAB1_SCHPO
AccessioniPrimary (citable) accession number: O59722
Secondary accession number(s): O43072
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 16, 2003
Last modified: May 11, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. 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.