Q3UQ44

SS
Gene name
Iqgap2
Protein name
Ras GTPase-activating-like protein IQGAP2
Names
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:544963
EC number
Protein Class

Descriptions

Ras GTPase-activating-like protein IQGAP1 plays a crucial role in regulating the dynamics and assembly of the actin cytoskeleton. IQGAP1 binds directly nucleotide-depleted Cdc42 (Cdc42-ND) and may serve as a negative effector or sequester nucleotide-free Cdc42 to prevent signaling. The regions C1 (956-1274) and C2 (1276-1657) of IQGAP1 can either interact with nucleotide-free Cdc42, or interact together, depending on the phosphorylation state of Ser-1443. When Ser-1443 is not phosphorylated, C1 and C2 interact, which prevents binding of nucleotide-free Cdc42 and promotes binding of GTP-bound Cdc42. The phosphorylation of Ser-1443 prevents interaction between C1 and C2, which opens the structure of the C-terminus and allows binding and sequestration of nucleotide-free Cdc42 on both C1 and C2.

Autoinhibitory domains (AIDs)

1189-1575 (C2 fragments) SS

Target domain

869-1187 (C1 fragments)

Relief mechanism

PTM

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q3UQ44

Entry ID Method Resolution Chain Position Source
AF-Q3UQ44-F1 Predicted AlphaFoldDB

80 variants for Q3UQ44

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3403824891 25 A>S No EVA
rs3403762906 38 Y>S No EVA
rs3389290580 70 R>L No EVA
rs3389309637 79 A>T No EVA
rs3389226695 141 N>T No EVA
rs3389226648 146 I>V No EVA
rs3389226709 147 Y>* No EVA
rs3389294672 155 Y>F No EVA
rs3389313511 166 Q>E No EVA
rs3389290588 180 S>I No EVA
rs3389309629 184 K>T No EVA
rs3389272531 215 H>Y No EVA
rs3389298771 228 G>R No EVA
rs3389265128 285 Y>* No EVA
rs3389294625 294 I>N No EVA
rs3389290591 350 N>S No EVA
rs3389293505 354 Q>R No EVA
rs3389299357 356 T>I No EVA
rs234561023 443 I>V No EVA
rs50650803 485 D>N No EVA
rs3389298801 501 T>S No EVA
rs3389293537 508 D>V No EVA
rs3389280938 510 K>N No EVA
rs29724564 513 S>F No EVA
rs3389272519 523 Q>* No EVA
rs29727558 526 N>D No EVA
rs1133124710 530 V>G No EVA
rs241095509 543 V>I No EVA
rs261510652 544 D>N No EVA
rs47890647 565 P>S No EVA
rs3389272480 643 I>T No EVA
rs3389280934 644 V>M No EVA
rs51782746 666 R>C No EVA
rs48301116 671 T>A No EVA
rs48735573 672 L>S No EVA
rs3389299381 693 S>I No EVA
rs3389298781 696 K>Q No EVA
rs3389294608 769 D>Y No EVA
rs3389296319 770 Y>N No EVA
rs3404533839 797 D>E No EVA
rs3404520987 798 F>I No EVA
rs3389290630 831 K>T No EVA
rs3404819253 950 K>M No EVA
rs3404520989 957 I>L No EVA
rs258829184 980 T>S No EVA
rs3389272530 997 A>V No EVA
rs3389313487 1000 I>N No EVA
rs3389265172 1013 N>I No EVA
rs49091994 1056 D>G No EVA
rs3389313527 1100 V>A No EVA
rs3389296340 1104 L>V No EVA
rs3389306198 1116 P>H No EVA
rs3389309672 1119 F>L No EVA
rs3389298772 1145 L>M No EVA
rs3508038489 1148 A>T No EVA
rs3389293546 1160 H>R No EVA
rs246182125 1186 P>L No EVA
rs3389306173 1198 T>M No EVA
rs3389306196 1231 T>S No EVA
rs3389290585 1233 K>R No EVA
rs3389290602 1265 N>I No EVA
rs3389299420 1281 S>P No EVA
rs51999239 1329 G>E No EVA
rs251313128 1344 V>I No EVA
rs47476195 1349 T>A No EVA
rs3389290593 1367 L>F No EVA
rs3389290577 1413 L>P No EVA
rs3389309655 1427 A>T No EVA
rs3389298824 1434 F>S No EVA
rs3389290639 1465 D>N No EVA
rs29248733 1468 A>T No EVA
rs3389306194 1489 K>N No EVA
rs1133153746 1492 L>P No EVA
rs255731848 1511 I>M No EVA
rs864280553 1515 D>N No EVA
rs3389280944 1521 V>I No EVA
rs3389299612 1523 S>T No EVA
rs3389299604 1524 K>N No EVA
rs3389296297 1527 G>D No EVA
rs3389270709 1545 Y>* No EVA

No associated diseases with Q3UQ44

2 regional properties for Q3UQ44

Type Name Position InterPro Accession
domain Gasdermin, pore forming domain 5 - 232 IPR040460
domain Gasdermin, PUB domain 249 - 376 IPR041263

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane
  • Nucleus
  • Cytoplasm
  • Apical cell membrane
  • Basolateral cell membrane
  • Subcellular distribution is regulated by the cell cycle, nuclear levels increase at G1/S phase (PubMed:20883816)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cell cortex The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.
cell surface The external part of the cell wall and/or plasma membrane.
filopodium Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
lamellipodium A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments.
microvillus Thin cylindrical membrane-covered projections on the surface of an animal cell containing a core bundle of actin filaments. Present in especially large numbers on the absorptive surface of intestinal cells.

6 GO annotations of molecular function

Name Definition
actin filament binding Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
Arp2/3 complex binding Binding to an Arp2/3 complex, a protein complex that contains two actin-related proteins, Arp2 and Arp3, and five novel proteins (ARPC1-5).
calmodulin binding Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
GTPase activator activity Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP.
phosphatidylinositol-3,4,5-trisphosphate binding Binding to phosphatidylinositol-3,4,5-trisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3', 4' and 5' positions.
small GTPase binding Binding to a small monomeric GTPase.

4 GO annotations of biological process

Name Definition
Arp2/3 complex-mediated actin nucleation The actin nucleation process in which actin monomers combine to form a new branch on the side of an existing actin filament; mediated by the Arp2/3 protein complex and its interaction with other proteins.
mitotic actomyosin contractile ring assembly actin filament organization Any actin filament organization that is involved in mitotic actomyosin contractile ring assembly.
regulation of actin cytoskeleton organization Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
thrombin-activated receptor signaling pathway A G protein-coupled receptor signaling pathway initiated by thrombin binding to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P46940 IQGAP1 Ras GTPase-activating-like protein IQGAP1 Homo sapiens (Human) EV
Q86VI3 IQGAP3 Ras GTPase-activating-like protein IQGAP3 Homo sapiens (Human) SS
Q13576 IQGAP2 Ras GTPase-activating-like protein IQGAP2 Homo sapiens (Human) SS
Q9JKF1 Iqgap1 Ras GTPase-activating-like protein IQGAP1 Mus musculus (Mouse) SS
10 20 30 40 50 60
MSAAEEVDGL GVVRPHYGSV LDNERLTAEE MDERRRQNVA YEYLCHLEEA KRWMEACLGE
70 80 90 100 110 120
DLPPTTELEE GLRNGVYLAK LGNFFSPKVV SLKKIYDREQ TRYKATGLHF RHTDNVIQWL
130 140 150 160 170 180
NAMDEIGLPK IFYPETTDIY DRKNMPRCIY CIHALSLYLF KLGLAPQIQD LYGKVDFTEE
190 200 210 220 230 240
EINNMKIELE KYGIQMPAFS KIGGILANEL SVDEAALHAA VIAINEAIDR RVAADTFTAL
250 260 270 280 290 300
KNPNAMLVNL EEGLAPTYQD VLYQAKQDKM TNAKNRTENS DRERDVYEEL LTQAEIQGNV
310 320 330 340 350 360
NKVNTSSALA NISLALEQGC AVTLLKALQS LALGLRGLQT QNSDWYMKQL QSDLQQKRQS
370 380 390 400 410 420
GQTDPLQKEE VQAGVDAANS AAQQYQRRLA AVAAINAAIQ KGIAEKTVLE LMNPEAQLPQ
430 440 450 460 470 480
VYPFAADLYQ KELATLQQQS PEHSLTHPEL TVAVEMLSSV ALINRALESG DMTTVWKQLS
490 500 510 520 530 540
SSVTGLTNIE EENCQRYLDE LMKLKAQAHA ENNAFITWND IQACVDHVNL VVHEEHERIL
550 560 570 580 590 600
AIGLINEALD EGDAQKTLQA LQIPAAKLEG VLAEVAQHYQ DTLIRAKREK AQETQDESAV
610 620 630 640 650 660
LWLDEIQGGI WQSNKDTQEA QRFALGISAI NEAVDSGDVG RTLSALRSPD VGLYGVIPEC
670 680 690 700 710 720
GETYQSDLAE AKKKRLAAGD NNSKWVKHWV KGGYHYYHNL ETQAGGWAEP PDFVQNSVQL
730 740 750 760 770 780
SREEIQSSIS GVTAAYNREQ LWLANEGLIT KLQACCRGYL VRQEFRSRMN FLKKQIPAIT
790 800 810 820 830 840
CIQSQWRGYK QKKAYQDRLA YLHSHKDEVV KIQSLARMHQ ARKRYRDRLQ YFRDHINDII
850 860 870 880 890 900
KIQAFIRANK ARDDYKTLIN AEDPPMIVVR KFVHLLDQSD QDFQEELDLM KMREEVITLI
910 920 930 940 950 960
RSNQQLENDL NLMDIKIGLL VKNKITLQDV VSHSKKLTKK NKEQLSDMMM INKQKGGLKA
970 980 990 1000 1010 1020
LSKEKREKLE AYQHLFYLLQ TNPTYLAKLI FQMPQNKSTK FMDSVIFTLY NYASNQREEY
1030 1040 1050 1060 1070 1080
LLLRLFQTAL QEEIKSKVDQ IQEIVTGNPT VIKMVVSFNR GARGQNALRQ ILAPVVKEIM
1090 1100 1110 1120 1130 1140
DDKSLNIKTD PVDIYKSWVN QMESQTGEAS KLPYDVTPEQ ALSHEEVKTR LDNSIRNMRA
1150 1160 1170 1180 1190 1200
VTDKFLSAIV SSVDKIPYGM RFIAKVLKDS LHEKFPDAGE DELLKIIGNL LYYRYMNPAI
1210 1220 1230 1240 1250 1260
VAPDAFDIID LSAGGQLTTD QRRNLGSIAK MLQHAASNKM FLGDNAHLSI INEYLSQSYQ
1270 1280 1290 1300 1310 1320
KFRRFFQVAC DVPELQDKFN VDEYSDLVTL TKPVIYISIG EIINTHTLLL DHQDAIAPEH
1330 1340 1350 1360 1370 1380
NDPIHELLDD LGEVPTIESL IGESCGNSND PNKEALAKTE VSLTLTNKFD VPGDENAEMD
1390 1400 1410 1420 1430 1440
ARTILLNTKR LIVDVIRFQP GETLTEILET PATNEQEAEH QRAMQRRAIR DAKTPDKMKK
1450 1460 1470 1480 1490 1500
SKPMKEDNNL SLQEKKEKIQ TGLKKLTELG TVDPKNRYQE LINDIAKDIR NQRRYRQRRK
1510 1520 1530 1540 1550 1560
AELVKLQQTY SALNSKATFY GEQVDYYKSY IKTCLDNLAS KGKVSKKPRE MKGKKSKKIS
1570 1580 1590 1600 1610 1620
LKYTAARLHE KGVLLEIEDL QANQFKNVIF EIGPTEEVGD FEVKAKFMGV QMETFMLHYQ
1630 1640 1650
DLLQLQYEGV AVMKLFDRAK VNVNLLIFLL NKKFYGK