CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021818
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ras GTPase-activating-like protein IQGAP1 
Protein Synonyms/Alias
  
Gene Name
 Iqgap1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
104DREQTRYKATGLHFRacetylation[1]
503RYLDELMKLKAQAHAubiquitination[2]
684AAGDNNSKWVKHWVKacetylation[1]
871PPMIVVRKFVHLLDQacetylation[1]
940HSKKLTKKNKEQLSDubiquitination[2]
968LSKEKREKLEAYQHLacetylation[1]
1088DDKSLNIKTDPVDIYacetylation[3]
1111SQTGEASKLPYDVTPubiquitination[2]
1144NMRAVTDKFLSAIVSacetylation[1]
1155AIVSSVDKIPYGMRFubiquitination[2]
1174LKDSLHEKFPDAGEDacetylation[1]
1389RTILLNTKRLIVDVIubiquitination[2]
1465KIQTGLKKLTELGTVubiquitination[2]
1475ELGTVDPKNRYQELIubiquitination[2]
1528GEQVDYYKSYIKTCLacetylation[1]
1528GEQVDYYKSYIKTCLubiquitination[2]
1532DYYKSYIKTCLDNLAacetylation[1]
1562KSKKISLKYTAARLHacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
 Binds to activated CDC42 but does not stimulate its GTPase activity. It associates with calmodulin. Could serve as an assembly scaffold for the organization of a multimolecular complex that would interface incoming signals to the reorganization of the actin cytoskeleton at the plasma membrane. May promote neurite outgrowth. 
Sequence Annotation
 DOMAIN 44 159 CH.
 DOMAIN 685 710 WW.
 DOMAIN 745 774 IQ 1.
 DOMAIN 775 804 IQ 2.
 DOMAIN 805 834 IQ 3.
 DOMAIN 835 864 IQ 4.
 DOMAIN 1004 1237 Ras-GAP.
 REGION 956 1274 C1.
 REGION 1276 1657 C2.
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 271 271 Phosphothreonine.
 MOD_RES 330 330 Phosphoserine (By similarity).  
Keyword
 Acetylation; Calmodulin-binding; Cell membrane; Complete proteome; Membrane; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1657 AA 
Protein Sequence
MSAAEEVDGL GVVRPHYGSV LDNERLTAEE MDERRRQNVA YEYLCHLEEA KRWMEACLGE 60
DLPPTTELEE GLRNGVYLAK LGNFFSPKVV SLKKIYDREQ TRYKATGLHF RHTDNVIQWL 120
NAMDEIGLPK IFYPETTDIY DRKNMPRCIY CIHALSLYLF KLGLAPQIQD LYGKVDFTEE 180
EINNMKIELE KYGIQMPAFS KIGGILANEL SVDEAALHAA VIAINEAIDR RVAADTFTAL 240
KNPNAMLVNL EEGLAPTYQD VLYQAKQDKM TNAKNRTENS DRERDVYEEL LTQAEIQGNV 300
NKVNTSSALA NISLALEQGC AVTLLKALQS LALGLRGLQT QNSDWYMKQL QSDLQQKRQS 360
GQTDPLQKEE VQAGVDAANS AAQQYQRRLA AVAAINAAIQ KGIAEKTVLE LMNPEAQLPQ 420
VYPFAADLYQ KELATLQQQS PEHSLTHPEL TVAVEMLSSV ALINRALESG DMTTVWKQLS 480
SSVTGLTNIE EENCQRYLDE LMKLKAQAHA ENNAFITWND IQACVDHVNL VVHEEHERIL 540
AIGLINEALD EGDAQKTLQA LQIPAAKLEG VLAEVAQHYQ DTLIRAKREK AQETQDESAV 600
LWLDEIQGGI WQSNKDTQEA QRFALGISAI NEAVDSGDVG RTLSALRSPD VGLYGVIPEC 660
GETYQSDLAE AKKKRLAAGD NNSKWVKHWV KGGYHYYHNL ETQAGGWAEP PDFVQNSVQL 720
SREEIQSSIS GVTAAYNREQ LWLANEGLIT KLQACCRGYL VRQEFRSRMN FLKKQIPAIT 780
CIQSQWRGYK QKKAYQDRLA YLHSHKDEVV KIQSLARMHQ ARKRYRDRLQ YFRDHINDII 840
KIQAFIRANK ARDDYKTLIN AEDPPMIVVR KFVHLLDQSD QDFQEELDLM KMREEVITLI 900
RSNQQLENDL NLMDIKIGLL VKNKITLQDV VSHSKKLTKK NKEQLSDMMM INKQKGGLKA 960
LSKEKREKLE AYQHLFYLLQ TNPTYLAKLI FQMPQNKSTK FMDSVIFTLY NYASNQREEY 1020
LLLRLFQTAL QEEIKSKVDQ IQEIVTGNPT VIKMVVSFNR GARGQNALRQ ILAPVVKEIM 1080
DDKSLNIKTD PVDIYKSWVN QMESQTGEAS KLPYDVTPEQ ALSHEEVKTR LDNSIRNMRA 1140
VTDKFLSAIV SSVDKIPYGM RFIAKVLKDS LHEKFPDAGE DELLKIIGNL LYYRYMNPAI 1200
VAPDAFDIID LSAGGQLTTD QRRNLGSIAK MLQHAASNKM FLGDNAHLSI INEYLSQSYQ 1260
KFRRFFQVAC DVPELQDKFN VDEYSDLVTL TKPVIYISIG EIINTHTLLL DHQDAIAPEH 1320
NDPIHELLDD LGEVPTIESL IGESCGNSND PNKEALAKTE VSLTLTNKFD VPGDENAEMD 1380
ARTILLNTKR LIVDVIRFQP GETLTEILET PATNEQEAEH QRAMQRRAIR DAKTPDKMKK 1440
SKPMKEDNNL SLQEKKEKIQ TGLKKLTELG TVDPKNRYQE LINDIAKDIR NQRRYRQRRK 1500
AELVKLQQTY SALNSKATFY GEQVDYYKSY IKTCLDNLAS KGKVSKKPRE MKGKKSKKIS 1560
LKYTAARLHE KGVLLEIEDL QANQFKNVIF EIGPTEEVGD FEVKAKFMGV QMETFMLHYQ 1620
DLLQLQYEGV AVMKLFDRAK VNVNLLIFLL NKKFYGK 1657 
Gene Ontology
 GO:0031252; C:cell leading edge; IGI:MGI.
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0016328; C:lateral plasma membrane; IDA:MGI.
 GO:0005874; C:microtubule; IEA:Compara.
 GO:0030496; C:midbody; IEA:Compara.
 GO:0043005; C:neuron projection; IGI:MGI.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0030529; C:ribonucleoprotein complex; IDA:MGI.
 GO:0036057; C:slit diaphragm; ISS:UniProtKB.
 GO:0005099; F:Ras GTPase activator activity; IEA:InterPro.
 GO:0071277; P:cellular response to calcium ion; IEA:Compara.
 GO:0072015; P:glomerular visceral epithelial cell development; ISS:UniProtKB.
 GO:0035305; P:negative regulation of dephosphorylation; IGI:MGI.
 GO:0045860; P:positive regulation of protein kinase activity; IMP:BHF-UCL.
 GO:0032320; P:positive regulation of Ras GTPase activity; IEA:GOC.
 GO:0001817; P:regulation of cytokine production; IMP:MGI.
 GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. 
Interpro
 IPR001715; CH-domain.
 IPR000048; IQ_motif_EF-hand-BS.
 IPR027401; Myosin-like_IQ_dom.
 IPR027417; P-loop_NTPase.
 IPR001936; RasGAP.
 IPR000593; RasGAP_C.
 IPR023152; RasGAP_CS.
 IPR008936; Rho_GTPase_activation_prot.
 IPR001202; WW_dom. 
Pfam
 PF00307; CH
 PF00612; IQ
 PF00616; RasGAP
 PF03836; RasGAP_C 
SMART
 SM00033; CH
 SM00015; IQ
 SM00323; RasGAP 
PROSITE
 PS50021; CH
 PS50096; IQ
 PS00509; RAS_GTPASE_ACTIV_1
 PS50018; RAS_GTPASE_ACTIV_2
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2 
PRINTS