Search Results

Overview

Uniprot IDQ9H2D6
Protein NameTRIO and F-actin-binding protein
Gene NameTRIOBP
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1917 STQKGPLKAGEQRAG
1971 RTPDRLAKQEELERD
1988 QRSEERRKWFEATDS

Function

Regulates actin cytoskeletal organization, cell spreading and cell contraction by directly binding and stabilizing filamentous F-actin and prevents its depolymerization (PubMed:18194665, PubMed:28438837). May also serve as a linker protein to recruit proteins required for F-actin formation and turnover (PubMed:18194665). Essential for correct mitotic progression (PubMed:22820163, PubMed:24692559)

Protein Sequence

10 MEEVPGDALC 20 EHFEANILTQ 30 NRCQNCFHPE 40 EAHGARYQEL 50 RSPSGAEVPY 60 CDLPRCPPAP 70 EDPLSASTSG 80 CQSVVDPGLR 90 PGPKRGPSPS 100 AGLPEEGPTA 110 APRSRSRELE 120 AVPYLEGLTT 130 SLCGSCNEDP 140 GSDPTSSPDS 150 ATPDDTSNSS 160 SVDWDTVERQ 170 EEEAPSWDEL 180 AVMIPRRPRE 190 GPRADSSQRA 200 PSLLTRSPVG 210 GDAAGQKKED 220 TGGGGRSAGQ 230 HWARLRGESG 240 LSLERHRSTL 250 TQASSMTPHS 260 GPRSTTSQAS 270 PAQRDTAQAA 280 STREIPRASS 290 PHRITQRDTS 300 RASSTQQEIS 310 RASSTQQETS 320 RASSTQEDTP 330 RASSTQEDTP 340 RASSTQWNTP 350 RASSPSRSTQ 360 LDNPRTSSTQ 370 QDNPQTSFPT 380 CTPQRENPRT 390 PCVQQDDPRA 400 SSPNRTTQRE 410 NSRTSCAQRD 420 NPKASRTSSP 430 NRATRDNPRT 440 SCAQRDNPRA 450 SSPSRATRDN 460 PTTSCAQRDN 470 PRASRTSSPN 480 RATRDNPRTS 490 CAQRDNPRAS 500 SPSRATRDNP 510 TTSCAQRDNP 520 RASRTSSPNR 530 ATRDNPRTSC 540 AQRDNPRASS 550 PNRAARDNPT 560 TSCAQRDNPR 570 ASRTSSPNRA 580 TRDNPRTSCA 590 QRDNPRASSP 600 NRATRDNPTT 610 SCAQRDNPRA 620 SRTSSPNRAT 630 RDNPRTSCAQ 640 RDNPRASSPN 650 RTTQQDSPRT 660 SCARRDDPRA 670 SSPNRTIQQE 680 NPRTSCALRD 690 NPRASSPSRT 700 IQQENPRTSC 710 AQRDDPRASS 720 PNRTTQQENP 730 RTSCARRDNP 740 RASSRNRTIQ 750 RDNPRTSCAQ 760 RDNPRASSPN 770 RTIQQENLRT 780 SCTRQDNPRT 790 SSPNRATRDN 800 PRTSCAQRDN 810 LRASSPIRAT 820 QQDNPRTCIQ 830 QNIPRSSSTQ 840 QDNPKTSCTK 850 RDNLRPTCTQ 860 RDRTQSFSFQ 870 RDNPGTSSSQ 880 CCTQKENLRP 890 SSPHRSTQWN 900 NPRNSSPHRT 910 NKDIPWASFP 920 LRPTQSDGPR 930 TSSPSRSKQS 940 EVPWASIALR 950 PTQGDRPQTS 960 SPSRPAQHDP 970 PQSSFGPTQY 980 NLPSRATSSS 990 HNPGHQSTSR 1000 TSSPVYPAAY 1010 GAPLTSPEPS 1020 QPPCAVCIGH 1030 RDAPRASSPP 1040 RYLQHDPFPF 1050 FPEPRAPESE 1060 PPHHEPPYIP 1070 PAVCIGHRDA 1080 PRASSPPRHT 1090 QFDPFPFLPD 1100 TSDAEHQCQS 1110 PQHEPLQLPA 1120 PVCIGYRDAP 1130 RASSPPRQAP 1140 EPSLLFQDLP 1150 RASTESLVPS 1160 MDSLHECPHI 1170 PTPVCIGHRD 1180 APSFSSPPRQ 1190 APEPSLFFQD 1200 PPGTSMESLA 1210 PSTDSLHGSP 1220 VLIPQVCIGH 1230 RDAPRASSPP 1240 RHPPSDLAFL 1250 APSPSPGSSG 1260 GSRGSAPPGE 1270 TRHNLEREEY 1280 TVLADLPPPR 1290 RLAQRQPGPQ 1300 AQCSSGGRTH 1310 SPGRAEVERL 1320 FGQERRKSEA 1330 AGAFQAQDEG 1340 RSQQPSQGQS 1350 QLLRRQSSPA 1360 PSRQVTMLPA 1370 KQAELTRRSQ 1380 AEPPHPWSPE 1390 KRPEGDRQLQ 1400 GSPLPPRTSA 1410 RTPERELRTQ 1420 RPLESGQAGP 1430 RQPLGVWQSQ 1440 EEPPGSQGPH 1450 RHLERSWSSQ 1460 EGGLGPGGWW 1470 GCGEPSLGAA 1480 KAPEGAWGGT 1490 SREYKESWGQ 1500 PEAWEEKPTH 1510 ELPRELGKRS 1520 PLTSPPENWG 1530 GPAESSQSWH 1540 SGTPTAVGWG 1550 AEGACPYPRG 1560 SERRPELDWR 1570 DLLGLLRAPG 1580 EGVWARVPSL 1590 DWEGLLELLQ 1600 ARLPRKDPAG 1610 HRDDLARALG 1620 PELGPPGTND 1630 VPEQESHSQP 1640 EGWAEATPVN 1650 GHSPALQSQS 1660 PVQLPSPACT 1670 STQWPKIKVT 1680 RGPATATLAG 1690 LEQTGPLGSR 1700 STAKGPSLPE 1710 LQFQPEEPEE 1720 SEPSRGQDPL 1730 TDQKQADSAD 1740 KRPAEGKAGS 1750 PLKGRLVTSW 1760 RMPGDRPTLF 1770 NPFLLSLGVL 1780 RWRRPDLLNF 1790 KKGWMSILDE 1800 PGEPPSPSLT 1810 TTSTSQWKKH 1820 WFVLTDSSLK 1830 YYRDSTAEEA 1840 DELDGEIDLR 1850 SCTDVTEYAV 1860 QRNYGFQIHT 1870 KDAVYTLSAM 1880 TSGIRRNWIE 1890 ALRKTVRPTS 1900 APDVTKLSDS 1910 NKENALHSYS 1920 TQKGPLKAGE 1930 QRAGSEVISR 1940 GGPRKADGQR 1950 QALDYVELSP 1960 LTQASPQRAR 1970 TPARTPDRLA 1980 KQEELERDLA 1990 QRSEERRKWF 2000 EATDSRTPEV 2010 PAGEGPRRGL 2020 GAPLTEDQQN 2030 RLSEEIEKKW 2040 QELEKLPLRE 2050 NKRVPLTALL 2060 NQSRGERRGP 2070 PSDGHEALEK 2080 EVQALRAQLE 2090 AWRLQGEAPQ 2100 SALRSQEDGH 2110 IPPGYISQEA 2120 CERSLAEMES 2130 SHQQVMEELQ 2140 RHHERELQRL 2150 QQEKEWLLAE 2160 ETAATASAIE 2170 AMKKAYQEEL 2180 SRELSKTRSL 2190 QQGPDGLRKQ 2200 HQSDVEALKR 2210 ELQVLSEQYS 2220 QKCLEIGALM 2230 RQAEEREHTL 2240 RRCQQEGQEL 2250 LRHNQELHGR 2260 LSEEIDQLRG 2270 FIASQGMGNG 2280 CGRSNERSSC 2290 ELEVLLRVKE 2300 NELQYLKKEV 2310 QCLRDELQMM 2320 QKDKRFTSGK 2330 YQDVYVELSH 2340 IKTRSEREIE 2350 QLKEHLRLAM 2360 AALQEKESMR NSLAE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0005813 centrosome
Cellular Component GO:0000781 chromosome, telomeric region
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0030496 midbody
Cellular Component GO:0005634 nucleus
Cellular Component GO:0120044 stereocilium base
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0045159 myosin II binding
Molecular Function GO:0031267 small GTPase binding
Molecular Function GO:0031625 ubiquitin protein ligase binding
Biological Process GO:0030047 actin modification
Biological Process GO:0051016 barbed-end actin filament capping
Biological Process GO:0051301 cell division
Biological Process GO:1900026 positive regulation of substrate adhesion-dependent cell spreading

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] 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.