O59722

PR
Gene name
fab1 (ste12, SPBC3E7.01, SPBC6B1.11c)
Protein name
1-phosphatidylinositol 3-phosphate 5-kinase fab1
Names
Phosphatidylinositol 3-phosphate 5-kinase, Diphosphoinositide kinase, Type III PIP kinase, PIPkin-III
Species
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
KEGG Pathway
spo:SPBC3E7.01
EC number
2.7.1.150: Phosphotransferases with an alcohol group as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

96-260 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for O59722

Entry ID Method Resolution Chain Position Source
AF-O59722-F1 Predicted AlphaFoldDB

No variants for O59722

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O59722

No associated diseases with O59722

No regional properties for O59722

Type Name Position InterPro Accession
No domain, repeats, and functional sites for O59722

Functions

Description
EC Number 2.7.1.150 Phosphotransferases with an alcohol group as acceptor
Subcellular Localization
  • Cytoplasm
  • During cell fusion of opposite mating types, migrates to the isthmus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
endosome membrane The lipid bilayer surrounding an endosome.
fungal-type vacuole membrane The lipid bilayer surrounding a vacuole, the shape of which correlates with cell cycle phase. The membrane separates its contents from the cytoplasm of the cell. An example of this structure is found in Saccharomyces cerevisiae.
PAS complex A class III phosphatidylinositol 3-kinase complex that contains a phosphatidylinositol-3-phosphate 5-kinase subunit (Fab1p in yeast; PIKfyve in mammals), a kinase activator, and a phosphatase, and may also contain additional proteins; it is involved in regulating the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate. In mammals the complex is composed of PIKFYVE, FIG4 and VAC14. In yeast it is composed of Atg18p, Fig4p, Fab1p, Vac14p and Vac7p.

4 GO annotations of molecular function

Name Definition
1-phosphatidylinositol-3-phosphate 5-kinase activity Catalysis of the reaction: a 1-phosphatidyl-1D-myo-inositol 3-phosphate + ATP = a 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + ADP + 2 H(+).
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
phosphatidylinositol-3-phosphate binding Binding to phosphatidylinositol-3-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' position.

3 GO annotations of biological process

Name Definition
phosphatidylinositol phosphate biosynthetic process The chemical reactions and pathways resulting in the formation of phosphatidylinositol phosphate.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
protein modification by small protein conjugation or removal A protein modification process in which one or more groups of a small protein, such as ubiquitin or a ubiquitin-like protein, are covalently attached to or removed from a target protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSEVETPTAA SPTFPVETSH RLDTLHTSST EQIIKDSENV VHTTLKLPTS TLSREFWMKD
70 80 90 100 110 120
ERTNNCSLCE TEFTLFRRKH HCRICGKIIC KYCLKEAPGF IFRLQGSIKV CRPCASILVN
130 140 150 160 170 180
NYSRSQLFNH SLNESKNRDL TEQHPFVTLD ELNSNDQVLS SFGDLSSTFE MPNNIHPPEV
190 200 210 220 230 240
APMIAIPSSR SNYDSPGWAH HSIFLDWSKR NLDSNVINVE DSESGKYNAL TITNSYDAGP
250 260 270 280 290 300
SSVSTDYRPV NFGKVPSYSK LRKNKAFSSA KVSDMYLSAD ERNRLEDFSK GDRGLSFVNL
310 320 330 340 350 360
SPNIKATSYD RLSTVINEPF ISRSSSLTDE RGLADSGNSY HHFSDSDDES LFNDGLGLSF
370 380 390 400 410 420
HANSAIIKQR QQNVASIQRY GNESYLSNFL KAFLPKTVCD YLFPSSTIPD GLPALIENFN
430 440 450 460 470 480
ARVDKVNHPG GTEEPLPYQG KSRASSVVTS SKSTCILPPW ILFSDSFNQL VCTFLGKLLF
490 500 510 520 530 540
QMLNDEGVDS PMQWVLCLPK ILLKMALDLG PDIRSGDDID VRSYVKIKKI PGGSIQDCFL
550 560 570 580 590 600
VNGVLFSKKA SSKSMDRSLR RPRIALLTFS LDYACDEQRI LSLDLIISQQ EEYIINLVNR
610 620 630 640 650 660
ICMLKPNLVF AQGQIPSIAL KYFEEHGVIA FHGLKESVLY DIARCCRADI ISSIDKLSLC
670 680 690 700 710 720
PRLGTCGRFQ LRTYVVDENK GLRKTFAILD RCSERLGCTI VLRGADYNQL SKVKKIVELV
730 740 750 760 770 780
VLIAYHIKLE CALLRDKFVN MPELFETTYQ SLSRKSLPSF ASTAADKEKS QNHEKKSLNS
790 800 810 820 830 840
DNQSLRPLEN ENQSVSSTQG SNSPLELINN LPASDDYSSI TKALKTRFLT FSPFLSKPLP
850 860 870 880 890 900
RLLNQVNYYQ FIRNKLLKDV KLHPYSPTGS FVMKQSENDN VEESYEESYK FFCIDERYHF
910 920 930 940 950 960
LEKQWTLYYS HSKLMFSPFS SQRIILLYSI INKETSVPCI GPERCLLEFY RETDCTLGQY
970 980 990 1000 1010 1020
IEDSCLNTNV SCGGEYCKTN DMLWHYRSYV HGNSRISVFL ESFSCPVPGL EEKIIMWSYC
1030 1040 1050 1060 1070 1080
KFCKKNTHIT VMSEETWKYS FGKYLEFMFY NSQIRDRFEF CDHSVMAQHV HYFGYCNMAL
1090 1100 1110 1120 1130 1140
RFQRDLIEIF ELFVPSVTLR NNPSYIKELK EKEYKRLKGV IEKCLSSVAS RINQIKCDWV
1150 1160 1170 1180 1190 1200
TDPEKFESCT SEISKFRTLL SSDYTELYSE FDSIYLNSST SDYLSLNSIL RVLQGKMVKW
1210 1220 1230 1240 1250 1260
EQRFLDYQRL YLPSYKELSK IAAAQIKKVF LERPLSQTPL DLPETLENTQ IDIYPSFKTE
1270 1280 1290 1300 1310 1320
STDDQLEKVT QTNVASNKRV APYADSMANV GSPESDCFSV ATSSDIPKAN IDFTNDISTQ
1330 1340 1350 1360 1370 1380
NTFPASPVSN SGFSRQTYPN ISQRQGVNML SHKRKSASTS DRRFVNASST SGMNMPISSS
1390 1400 1410 1420 1430 1440
ISAKISSIQN STKYSPRKPI PAKDVRVSSL VRRFEELSLQ LQEKQKRDEE LIKARRKRAL
1450 1460 1470 1480 1490 1500
PVVPSKPVVE VFNDLNEAFD DENSEDENGI NDTKENRATE SNFSGVDSMS KERENVSSNE
1510 1520 1530 1540 1550 1560
DNSPEAFEDI FGILFKNESG LEEQQNLEPS SQMDKEGSKL PTSGPLADKT SVYRILSAFW
1570 1580 1590 1600 1610 1620
NEWNSLNPPP FEFPLQPTEH MFSDSNVIIR EDEPSSLISF TLSSPDYLSK MVEIEDSMDE
1630 1640 1650 1660 1670 1680
ALTNQGLQGS TQFKIENLML KPTGTHLKYQ FEEGSARLSC KVFFAEQFSA LRRACGCEET
1690 1700 1710 1720 1730 1740
FVTSLARCSL WESSGGKSGS AFLKTFDKKY ILKVLSRLES DSLLNFAPAY FDYISKVFFH
1750 1760 1770 1780 1790 1800
ELPTALTKIF GFYRVDIRNP TTGTICKTDI MIMENVFYDE CPSRIFDLKG SMRNRHVEST
1810 1820 1830 1840 1850 1860
GKVDEVLLDE NLVELIYESP IFVSEQLKSL LHSCLWNDTL FLSKLNIMDY SLIVGIDYTK
1870 1880 1890 1900 1910 1920
KELYVGIIDF IRTYTWDKKL ESWVKEKGLV GRGPEPTIVT PKQYKNRFRK AMDCYILASQ
1930
DFETGEGFKF CE