Search Results

Overview

Uniprot IDO15056
Protein NamePolyphosphatidylinositol phosphatase SYNJ2
Gene NameSYNJ2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1154 GAPQQPPKARTGISK

Function

Phosphatase that hydrolyzes phosphate groups from the inositol ring of phosphoinositides and inositol phosphates, in a domain-specific manner (PubMed:11084340, PubMed:12699622, PubMed:40969890). The 5-PPase domain catalyzes removal of the 5-phosphate from substrates such as phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3), inositol-1,4,5-trisphosphate (Ins(1,4,5)P3) and inositol-1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4) (PubMed:11084340, PubMed:12699622, PubMed:40969890). The SAC domain hydrolyzes phosphates at the 3- and 4-positions of the inositol ring, targeting phosphatidylinositol-3-phosphate (PI(3)P), phosphatidylinositol-4-phosphate (PI(4)P), and phosphatidylinositol-3,5-bisphosphate (PI(3,5)P2) (By similarity). Plays a role in the phosphatidylinositol metabolic process during the early stage of clathrin-coated-pit formation (PubMed:12699622). During EGF activation, plays a role in receptor-mediated endocytosis (RME) by converting PtdIns(4,5)P2 to PtdIns(4)P through the H2O2-dependent oxidation of the 4-phosphatase domain (By similarity). May play a role in tumor cell invadopodia formation (PubMed:23076136)

Protein Sequence

10 MALSKGLRLL 20 GRLGAEGDCS 30 VLLEARGRDD 40 CLLFEAGTVA 50 TLAPEEKEVI 60 KGQYGKLTDA 70 YGCLGELRLK 80 SGGTSLSFLV 90 LVTGCTSVGR 100 IPDAEIYKIT 110 ATDFYPLQEE 120 AKEEERLIAL 130 KKILSSGVFY 140 FSWPNDGSRF 150 DLTVRTQKQG 160 DDSSEWGNSF 170 FWNQLLHVPL 180 RQHQVSCCDW 190 LLKIICGVVT 200 IRTVYASHKQ 210 AKACLVSRVS 220 CERTGTRFHT 230 RGVNDDGHVS 240 NFVETEQMIY 250 MDDGVSSFVQ 260 IRGSVPLFWE 270 QPGLQVGSHH 280 LRLHRGLEAN 290 APAFDRHMVL 300 LKEQYGQQVV 310 VNLLGSRGGE 320 EVLNRAFKKL 330 LWASCHAGDT 340 PMINFDFHQF 350 AKGGKLEKLE 360 TLLRPQLKLH 370 WEDFDVFTKG 380 ENVSPRFQKG 390 TLRMNCLDCL 400 DRTNTVQSFI 410 ALEVLHLQLK 420 TLGLSSKPIV 430 DRFVESFKAM 440 WSLNGHSLSK 450 VFTGSRALEG 460 KAKVGKLKDG 470 ARSMSRTIQS 480 NFFDGVKQEA 490 IKLLLVGDVY 500 GEEVADKGGM 510 LLDSTALLVT 520 PRILKAMTER 530 QSEFTNFKRI 540 RIAMGTWNVN 550 GGKQFRSNVL 560 RTAELTDWLL 570 DSPQLSGATD 580 SQDDSSPADI 590 FAVGFEEMVE 600 LSAGNIVNAS 610 TTNKKMWGEQ 620 LQKAISRSHR 630 YILLTSAQLV 640 GVCLYIFVRP 650 YHVPFIRDVA 660 IDTVKTGMGG 670 KAGNKGAVGI 680 RFQFHSTSFC 690 FICSHLTAGQ 700 SQVKERNEDY 710 KEITQKLCFP 720 MGRNVFSHDY 730 VFWCGDFNYR 740 IDLTYEEVFY 750 FVKRQDWKKL 760 LEFDQLQLQK 770 SSGKIFKDFH 780 EGAINFGPTY 790 KYDVGSAAYD 800 TSDKCRTPAW 810 TDRVLWWRKK 820 HPFDKTAGEL 830 NLLDSDLDVD 840 TKVRHTWSPG 850 ALQYYGRAEL 860 QASDHRPVLA 870 IVEVEVQEVD 880 VGARERVFQE 890 VSSFQGPLDA 900 TVVVNLQSPT 910 LEEKNEFPED 920 LRTELMQTLG 930 SYGTIVLVRI 940 NQGQMLVTFA 950 DSHSALSVLD 960 VDGMKVKGRA 970 VKIRPKTKDW 980 LKGLREEIIR 990 KRDSMAPVSP 1000 TANSCLLEEN 1010 FDFTSLDYES 1020 EGDILEDDED 1030 YLVDEFNQPG 1040 VSDSELGGDD 1050 LSDVPGPTAL 1060 APPSKSPALT 1070 KKKQHPTYKD 1080 DADLVELKRE 1090 LEAVGEFRHR 1100 SPSRSLSVPN 1110 RPRPPQPPQR 1120 PPPPTGLMVK 1130 KSASDASISS 1140 GTHGQYSILQ 1150 TARLLPGAPQ 1160 QPPKARTGIS 1170 KPYNVKQIKT 1180 TNAQEAEAAI 1190 RCLLEARGGA 1200 SEEALSAVAP 1210 RDLEASSEPE 1220 PTPGAAKPET 1230 PQAPPLLPRR 1240 PPPRVPAIKK 1250 PTLRRTGKPL 1260 SPEEQFEQQT 1270 VHFTIGPPET 1280 SVEAPPVVTA 1290 PRVPPVPKPR 1300 TFQPGKAAER 1310 PSHRKPASDE 1320 APPGAGASVP 1330 PPLEAPPLVP 1340 KVPPRRKKSA 1350 PAAFHLQVLQ 1360 SNSQLLQGLT 1370 YNSSDSPSGH 1380 PPAAGTVFPQ 1390 GDFLSTSSAT 1400 SPDSDGTKAM 1410 KPEAAPLLGD 1420 YQDPFWNLLH 1430 HPKLLNNTWL 1440 SKSSDPLDSG 1450 TRSPKRDPID 1460 PVSAGASAAK 1470 AELPPDHEHK 1480 TLGHWVTISD 1490 QEKRTALQVF DPLAKT

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005856 cytoskeleton
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016020 membrane
Cellular Component GO:0045121 membrane raft
Cellular Component GO:0048471 perinuclear region of cytoplasm
Cellular Component GO:0098793 presynapse
Cellular Component GO:0032587 ruffle membrane
Molecular Function GO:0052658 inositol-1,4,5-trisphosphate 5-phosphatase activity
Molecular Function GO:0034596 phosphatidylinositol phosphate 4-phosphatase activity
Molecular Function GO:0034485 phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity
Molecular Function GO:0052629 phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity
Molecular Function GO:0043813 phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity
Molecular Function GO:0004438 phosphatidylinositol-3-phosphate phosphatase activity
Molecular Function GO:0004439 phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity
Molecular Function GO:0043812 phosphatidylinositol-4-phosphate phosphatase activity
Molecular Function GO:0003723 RNA binding
Biological Process GO:0048268 clathrin coat assembly
Biological Process GO:0061024 membrane organization
Biological Process GO:0006661 phosphatidylinositol biosynthetic process
Biological Process GO:0046856 phosphatidylinositol dephosphorylation
Biological Process GO:0046488 phosphatidylinositol metabolic process
Biological Process GO:0006898 receptor-mediated endocytosis
Biological Process GO:0048488 synaptic vesicle endocytosis

Reference

[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.