Search Results

Overview

Uniprot IDP46940
Protein NameRas GTPase-activating-like protein IQGAP1
Gene NameIQGAP1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1027 YLLLRLFKTALQEEI
104 DREQTRYKATGLHFR
1389 RTILLNTKRLIVDVI
1445 MKKSKSVKEDSNLTL
1455 SNLTLQEKKEKIQTG
1456 NLTLQEKKEKIQTGL
1475 ELGTVDPKNKYQELI
1477 GTVDPKNKYQELIND
1541 CLDNLASKGKVSKKP
1543 DNLASKGKVSKKPRE
1562 KSKKISLKYTAARLH
1571 TAARLHEKGVLLEIE
401 LINAAIQKGVAEKTV
924 IGLLVKNKITLQDVV
942 KKLTKKNKEQLSDMM
953 SDMMMINKQKGGLKA
959 NKQKGGLKALSKEKR
997 IFQMPQNKSTKFMDS

Function

Plays a crucial role in regulating the dynamics and assembly of the actin cytoskeleton. Recruited to the cell cortex by interaction with ILK which allows it to cooperate with its effector DIAPH1 to locally stabilize microtubules and allow stable insertion of caveolae into the plasma membrane (By similarity). Binds to activated CDC42 but does not stimulate its GTPase activity. Associates with calmodulin. May promote neurite outgrowth (PubMed:15695813). May play a possible role in cell cycle regulation by contributing to cell cycle progression after DNA replication arrest (PubMed:20883816)

Protein Sequence

10 MSAADEVDGL 20 GVARPHYGSV 30 LDNERLTAEE 40 MDERRRQNVA 50 YEYLCHLEEA 60 KRWMEACLGE 70 DLPPTTELEE 80 GLRNGVYLAK 90 LGNFFSPKVV 100 SLKKIYDREQ 110 TRYKATGLHF 120 RHTDNVIQWL 130 NAMDEIGLPK 140 IFYPETTDIY 150 DRKNMPRCIY 160 CIHALSLYLF 170 KLGLAPQIQD 180 LYGKVDFTEE 190 EINNMKTELE 200 KYGIQMPAFS 210 KIGGILANEL 220 SVDEAALHAA 230 VIAINEAIDR 240 RIPADTFAAL 250 KNPNAMLVNL 260 EEPLASTYQD 270 ILYQAKQDKM 280 TNAKNRTENS 290 ERERDVYEEL 300 LTQAEIQGNI 310 NKVNTFSALA 320 NIDLALEQGD 330 ALALFRALQS 340 PALGLRGLQQ 350 QNSDWYLKQL 360 LSDKQQKRQS 370 GQTDPLQKEE 380 LQSGVDAANS 390 AAQQYQRRLA 400 AVALINAAIQ 410 KGVAEKTVLE 420 LMNPEAQLPQ 430 VYPFAADLYQ 440 KELATLQRQS 450 PEHNLTHPEL 460 SVAVEMLSSV 470 ALINRALESG 480 DVNTVWKQLS 490 SSVTGLTNIE 500 EENCQRYLDE 510 LMKLKAQAHA 520 ENNEFITWND 530 IQACVDHVNL 540 VVQEEHERIL 550 AIGLINEALD 560 EGDAQKTLQA 570 LQIPAAKLEG 580 VLAEVAQHYQ 590 DTLIRAKREK 600 AQEIQDESAV 610 LWLDEIQGGI 620 WQSNKDTQEA 630 QKFALGIFAI 640 NEAVESGDVG 650 KTLSALRSPD 660 VGLYGVIPEC 670 GETYHSDLAE 680 AKKKKLAVGD 690 NNSKWVKHWV 700 KGGYYYYHNL 710 ETQEGGWDEP 720 PNFVQNSMQL 730 SREEIQSSIS 740 GVTAAYNREQ 750 LWLANEGLIT 760 RLQARCRGYL 770 VRQEFRSRMN 780 FLKKQIPAIT 790 CIQSQWRGYK 800 QKKAYQDRLA 810 YLRSHKDEVV 820 KIQSLARMHQ 830 ARKRYRDRLQ 840 YFRDHINDII 850 KIQAFIRANK 860 ARDDYKTLIN 870 AEDPPMVVVR 880 KFVHLLDQSD 890 QDFQEELDLM 900 KMREEVITLI 910 RSNQQLENDL 920 NLMDIKIGLL 930 VKNKITLQDV 940 VSHSKKLTKK 950 NKEQLSDMMM 960 INKQKGGLKA 970 LSKEKREKLE 980 AYQHLFYLLQ 990 TNPTYLAKLI 1000 FQMPQNKSTK 1010 FMDSVIFTLY 1020 NYASNQREEY 1030 LLLRLFKTAL 1040 QEEIKSKVDQ 1050 IQEIVTGNPT 1060 VIKMVVSFNR 1070 GARGQNALRQ 1080 ILAPVVKEIM 1090 DDKSLNIKTD 1100 PVDIYKSWVN 1110 QMESQTGEAS 1120 KLPYDVTPEQ 1130 ALAHEEVKTR 1140 LDSSIRNMRA 1150 VTDKFLSAIV 1160 SSVDKIPYGM 1170 RFIAKVLKDS 1180 LHEKFPDAGE 1190 DELLKIIGNL 1200 LYYRYMNPAI 1210 VAPDAFDIID 1220 LSAGGQLTTD 1230 QRRNLGSIAK 1240 MLQHAASNKM 1250 FLGDNAHLSI 1260 INEYLSQSYQ 1270 KFRRFFQTAC 1280 DVPELQDKFN 1290 VDEYSDLVTL 1300 TKPVIYISIG 1310 EIINTHTLLL 1320 DHQDAIAPEH 1330 NDPIHELLDD 1340 LGEVPTIESL 1350 IGESSGNLND 1360 PNKEALAKTE 1370 VSLTLTNKFD 1380 VPGDENAEMD 1390 ARTILLNTKR 1400 LIVDVIRFQP 1410 GETLTEILET 1420 PATSEQEAEH 1430 QRAMQRRAIR 1440 DAKTPDKMKK 1450 SKSVKEDSNL 1460 TLQEKKEKIQ 1470 TGLKKLTELG 1480 TVDPKNKYQE 1490 LINDIARDIR 1500 NQRRYRQRRK 1510 AELVKLQQTY 1520 AALNSKATFY 1530 GEQVDYYKSY 1540 IKTCLDNLAS 1550 KGKVSKKPRE 1560 MKGKKSKKIS 1570 LKYTAARLHE 1580 KGVLLEIEDL 1590 QVNQFKNVIF 1600 EISPTEEVGD 1610 FEVKAKFMGV 1620 QMETFMLHYQ 1630 DLLQLQYEGV 1640 AVMKLFDRAK 1650 VNVNLLIFLL NKKFYGK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005884 actin filament
Cellular Component GO:0016324 apical plasma membrane
Cellular Component GO:0030424 axon
Cellular Component GO:0016323 basolateral plasma membrane
Cellular Component GO:0005938 cell cortex
Cellular Component GO:0030054 cell junction
Cellular Component GO:0030864 cortical actin cytoskeleton
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0036464 cytoplasmic ribonucleoprotein granule
Cellular Component GO:0009898 cytoplasmic side of plasma membrane
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0030426 growth cone
Cellular Component GO:0016328 lateral plasma membrane
Cellular Component GO:0005874 microtubule
Cellular Component GO:0030496 midbody
Cellular Component GO:0043005 neuron projection
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:1990904 ribonucleoprotein complex
Cellular Component GO:0001726 ruffle
Cellular Component GO:0030667 secretory granule membrane
Cellular Component GO:0036057 slit diaphragm
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0005509 calcium ion binding
Molecular Function GO:0005516 calmodulin binding
Molecular Function GO:0005096 GTPase activator activity
Molecular Function GO:0005095 GTPase inhibitor activity
Molecular Function GO:0005078 MAP-kinase scaffold activity
Molecular Function GO:0060090 molecular adaptor activity
Molecular Function GO:0005547 phosphatidylinositol-3,4,5-trisphosphate binding
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0019901 protein kinase binding
Molecular Function GO:0019903 protein phosphatase binding
Molecular Function GO:0043539 protein serine/threonine kinase activator activity
Molecular Function GO:0044548 S100 protein binding
Molecular Function GO:0031267 small GTPase binding
Biological Process GO:0070836 caveola assembly
Biological Process GO:0016477 cell migration
Biological Process GO:0071277 cellular response to calcium ion
Biological Process GO:0071364 cellular response to epidermal growth factor stimulus
Biological Process GO:0036120 cellular response to platelet-derived growth factor stimulus
Biological Process GO:0007173 epidermal growth factor receptor signaling pathway
Biological Process GO:0008543 fibroblast growth factor receptor signaling pathway
Biological Process GO:0010761 fibroblast migration
Biological Process GO:1903479 mitotic actomyosin contractile ring assembly actin filament organization
Biological Process GO:0048008 platelet-derived growth factor receptor signaling pathway
Biological Process GO:0072015 podocyte development
Biological Process GO:0043410 positive regulation of MAPK cascade
Biological Process GO:0032956 regulation of actin cytoskeleton organization
Biological Process GO:0007346 regulation of mitotic cell cycle
Biological Process GO:0007165 signal transduction

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[6] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[7] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[8] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[9] 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.