※ dbPPT Protein Information

TagContent
UniProt Accession
Theoretical PI
5.27 
Molecular Weight
164758.58 
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Putative 1-phosphatidylinositol-3-phosphate 5-kinase FAB1D; Phosphatidylinositol 3-phosphate 5-kinase; Phosphatidylinositol 3-phosphate 5-kinase type III; PIPkin-III; Type III PIP kinase; Protein FORMS APLOID AND BINUCLEATE CELLS 1D 
Gene Name
FAB1D; At1g34260; F23M19.8 
Created Date
2013-04-03 
Organism
Arabidopsis thaliana(Mouse-ear cress) 
NCBI Taxa ID
3702 
Phosphorylation Sites
Position
Peptide
Source
References
84
VENVQFLSDREDDSD
dbPPT, P3DB, PhosPhAt
[4, 7]
135
ASLLGELSDESSEKR
dbPPT, P3DB, PhosPhAt
[2, 3, 5, 6]
15
SSSERSLSGECSVDG
dbPPT, P3DB, PhosPhAt
[1]
Functional Description
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate (By similarity). 
Sequence Annotation
chain 1 1456 Putative 1-phosphatidylinositol-3-phosphate 5-kinase FAB1D
domain 1115 1443 PIPK
compositionally biased region 114 118 Poly-Asp
Keyword
ATP-binding,Complete proteome,Kinase,Nucleotide-binding,Reference proteome,Transferase 
Sequence Source
UniProt 
Protein Sequence
MTPSNSLSSS ERSLSGECSV DGNSCDRGIE DECSSHSSQE DVELTKEVKV DRLERKSKSM 60
PSDILDILDE KSKENSVENV QFLSDREDDS DDVPVWEPPE PENPEDEVDG VFADDDDDCC 120
DGSKWNKASL LGELSDESSE KRKVYEENRR VMLEEADSKF KFIVSQLIKS AGFSIEESGY 180
WFEIVARLCW EAASMLKPAI DGKSVDPTEY IKVKCIATGS CVDSEVFKGL VFKKHAALKH 240
MATKYEHPRI MLVEGVLGHP ISGFSSLQSV NQDNEYLLKY VKPVVDIIEA SKPDVMLVEK 300
SVSRDIQKTI LDKGVTLVFD MKLHRLQRIS RCIGSPILSV DSLSSQKLKH CDSFRIEKIV 360
EEHNAAGESD KKPTKTLMFL EGCPTRLGCT ILLKGCHSER LKKVKEVVQY SFILAYHLML 420
EASFLADRHT MFSTIFAKEA TSCVVEIENF SPSPSPRESP SEAVDIPVSN GFDEQTIQIN 480
GEADGEKVGT WESDGDHVFS HEPYNPVIFT GFSSLSARLS KYLGFVQNPE SVPVSVDTDV 540
STTSNLDSIR ESEEDTAEKN EDKQPLLLDP ELPVNSSSDD GDNKSQTEND IESTLESQSI 600
LVLVSKRNAL RGIMCDQRHF SHIKFYKHFD VPLEKFLRDM FNQRNLCQTC VEFPEAHLYY 660
YAHQNKQLTI QIKRIPVAKG LAGEAKGKIW MWSRCGKCKT KNASRKSTKR VLISTAARSL 720
SFGKFLELSF SQQTFLNRSS SCGHSFDSDF LHFFGLGSMV AMLSYSQVAS YTVSLPPMKL 780
ESSILIKAGW LEKEFQTVFT KGISLFEDAA GFLKRLRSQF TNSDLRYQRA RKLLSNIEEL 840
LKHERCIFEE NIKNSFDKAK TIDDVSHRLL RLNRMRWELL LQALIWNYRL QSLVLSDRLL 900
PSSDETKIYE QGLKTVSEAG MTRYENDNKV SDSGSNGGID TPLVEHKDIP IAGASVGDND 960
QMAESYVPED NESQTLCSSS PDTTSPINNH FDTHLAVNVH STNGQEADKS IPVTGESLDD 1020
EVSTSNGPHI LGWDEWFWLP FEELRSKRIV DIEKEYLLKF EYVNNFTQEN LQTVNQIITE 1080
ESSRLRISLR DDDFIVSDYE DELSSLIACA LAHLNNEESK KPLSRCIHGS LQGFLDNNQD 1140
SKQTDRDVSR FSSESTNRLE TLPPPEVLVT FGSVKSVGKP KYSIVSLYAD DFRDLRKRCC 1200
SSELDYIASL SRCKPWDAKG GKSKSVFAKT LDDRFIVKEI KKTEYESFVT FATEYFKYMK 1260
DSYDLGNQTC LAKVLGIHQV TVRQPKGGGK EIRHDLMVME NLSFSRKVTR QYDLKGALHA 1320
RFTATSANGE DDVLLDQNFV NDMNKSPLYV SKTSKQNLQR AVYNDTSFLT SINVMDYSLL 1380
VGVDDENHEL VCGIIDYLRQ YTWDKQLETW VKSSLVVPKN VQPTVISPID YKTRFRKFMK 1440
THFLCVPDQW CDQGDS 1456 
Gene Ontology
GO:0000285; F: 1-phosphatidylinositol-3-phosphate 5-kinase activity; IEA: UniProtKB-EC
GO:0005524; F: ATP binding; IEA: UniProtKB-KW
GO:0044267; P: cellular protein metabolic process; IEA: InterPro 
Interpro
InterPro; IPR002423; Cpn60/TCP-1
InterPro; IPR027409; GroEL-like_apical_dom
InterPro; IPR027483; PInositol-4-P-5-kinase_C
InterPro; IPR002498; PInositol-4-P-5-kinase_core
InterPro; IPR027484; PInositol-4-P-5-kinase_N
Pfam
Pfam; PF00118; Cpn60_TCP1
Pfam; PF01504; PIP5K 
SMART
 
PROSITE
PS51455; PIPK 
PRINTS