CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007857
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ras GTPase-activating-like protein IQGAP1 
Protein Synonyms/Alias
 p195 
Gene Name
 IQGAP1 
Gene Synonyms/Alias
 KIAA0051 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
88LGNFFSPKVVSLKKIubiquitination[1, 2, 3]
348QNSDWYLKQLLSDKQubiquitination[1, 3]
503RYLDELMKLKAQAHAubiquitination[1, 3]
556LDEGDAQKTLQALQIubiquitination[4, 5, 6]
687DNNSKWVKHWVKGGYubiquitination[2]
811SHKDEVVKIQSLARMubiquitination[1, 2, 3, 7]
922IKIGLLVKNKITLQDubiquitination[2]
924IGLLVKNKITLQDVVubiquitination[2]
936DVVSHSKKLTKKNKEubiquitination[2]
940HSKKLTKKNKEQLSDubiquitination[2, 8]
942KKLTKKNKEQLSDMMubiquitination[2, 6, 9]
953SDMMMINKQKGGLKAubiquitination[1, 2, 3]
959NKQKGGLKALSKEKRubiquitination[2]
997IFQMPQNKSTKFMDSubiquitination[1, 3]
1027YLLLRLFKTALQEEIubiquitination[2, 9]
1088DDKSLNIKTDPVDIYubiquitination[1, 2, 3, 6]
1111SQTGEASKLPYDVTPubiquitination[2, 6, 9]
1144NMRAVTDKFLSAIVSubiquitination[1, 3]
1155AIVSSVDKIPYGMRFubiquitination[1, 2, 3]
1165YGMRFIAKVLKDSLHubiquitination[1, 3]
1230RNLGSIAKMLQHAASubiquitination[1, 3]
1389RTILLNTKRLIVDVIubiquitination[2]
1442PDKMKKSKSVKEDSNubiquitination[2, 6]
1445MKKSKSVKEDSNLTLubiquitination[6, 9]
1465KIQTGLKKLTELGTVubiquitination[2, 9]
1475ELGTVDPKNKYQELIubiquitination[2, 6, 9]
1477GTVDPKNKYQELINDubiquitination[1, 2, 3, 6]
1528GEQVDYYKSYIKTCLubiquitination[1, 2, 3, 6, 7, 9]
1532DYYKSYIKTCLDNLAubiquitination[2]
1562KSKKISLKYTAARLHubiquitination[1, 3]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [5] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [8] 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]
 [9] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
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 679 712 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.
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 271 271 Phosphothreonine (By similarity).
 MOD_RES 330 330 Phosphoserine.
 MOD_RES 1441 1441 Phosphoserine; by PKC (Probable).
 MOD_RES 1443 1443 Phosphoserine; by PKC/PRKCE.  
Keyword
 3D-structure; Acetylation; Calmodulin-binding; Cell membrane; Complete proteome; Direct protein sequencing; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1657 AA 
Protein Sequence
MSAADEVDGL GVARPHYGSV LDNERLTAEE MDERRRQNVA YEYLCHLEEA KRWMEACLGE 60
DLPPTTELEE GLRNGVYLAK LGNFFSPKVV SLKKIYDREQ TRYKATGLHF RHTDNVIQWL 120
NAMDEIGLPK IFYPETTDIY DRKNMPRCIY CIHALSLYLF KLGLAPQIQD LYGKVDFTEE 180
EINNMKTELE KYGIQMPAFS KIGGILANEL SVDEAALHAA VIAINEAIDR RIPADTFAAL 240
KNPNAMLVNL EEPLASTYQD ILYQAKQDKM TNAKNRTENS ERERDVYEEL LTQAEIQGNI 300
NKVNTFSALA NIDLALEQGD ALALFRALQS PALGLRGLQQ QNSDWYLKQL LSDKQQKRQS 360
GQTDPLQKEE LQSGVDAANS AAQQYQRRLA AVALINAAIQ KGVAEKTVLE LMNPEAQLPQ 420
VYPFAADLYQ KELATLQRQS PEHNLTHPEL SVAVEMLSSV ALINRALESG DVNTVWKQLS 480
SSVTGLTNIE EENCQRYLDE LMKLKAQAHA ENNEFITWND IQACVDHVNL VVQEEHERIL 540
AIGLINEALD EGDAQKTLQA LQIPAAKLEG VLAEVAQHYQ DTLIRAKREK AQEIQDESAV 600
LWLDEIQGGI WQSNKDTQEA QKFALGIFAI NEAVESGDVG KTLSALRSPD VGLYGVIPEC 660
GETYHSDLAE AKKKKLAVGD NNSKWVKHWV KGGYYYYHNL ETQEGGWDEP PNFVQNSMQL 720
SREEIQSSIS GVTAAYNREQ LWLANEGLIT RLQARCRGYL VRQEFRSRMN FLKKQIPAIT 780
CIQSQWRGYK QKKAYQDRLA YLRSHKDEVV KIQSLARMHQ ARKRYRDRLQ YFRDHINDII 840
KIQAFIRANK ARDDYKTLIN AEDPPMVVVR KFVHLLDQSD QDFQEELDLM KMREEVITLI 900
RSNQQLENDL NLMDIKIGLL VKNKITLQDV VSHSKKLTKK NKEQLSDMMM INKQKGGLKA 960
LSKEKREKLE AYQHLFYLLQ TNPTYLAKLI FQMPQNKSTK FMDSVIFTLY NYASNQREEY 1020
LLLRLFKTAL QEEIKSKVDQ IQEIVTGNPT VIKMVVSFNR GARGQNALRQ ILAPVVKEIM 1080
DDKSLNIKTD PVDIYKSWVN QMESQTGEAS KLPYDVTPEQ ALAHEEVKTR LDSSIRNMRA 1140
VTDKFLSAIV SSVDKIPYGM RFIAKVLKDS LHEKFPDAGE DELLKIIGNL LYYRYMNPAI 1200
VAPDAFDIID LSAGGQLTTD QRRNLGSIAK MLQHAASNKM FLGDNAHLSI INEYLSQSYQ 1260
KFRRFFQTAC DVPELQDKFN VDEYSDLVTL TKPVIYISIG EIINTHTLLL DHQDAIAPEH 1320
NDPIHELLDD LGEVPTIESL IGESSGNLND PNKEALAKTE VSLTLTNKFD VPGDENAEMD 1380
ARTILLNTKR LIVDVIRFQP GETLTEILET PATSEQEAEH QRAMQRRAIR DAKTPDKMKK 1440
SKSVKEDSNL TLQEKKEKIQ TGLKKLTELG TVDPKNKYQE LINDIARDIR NQRRYRQRRK 1500
AELVKLQQTY AALNSKATFY GEQVDYYKSY IKTCLDNLAS KGKVSKKPRE MKGKKSKKIS 1560
LKYTAARLHE KGVLLEIEDL QVNQFKNVIF EISPTEEVGD FEVKAKFMGV QMETFMLHYQ 1620
DLLQLQYEGV AVMKLFDRAK VNVNLLIFLL NKKFYGK 1657 
Gene Ontology
 GO:0005884; C:actin filament; TAS:ProtInc.
 GO:0031252; C:cell leading edge; IEA:Compara.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0016328; C:lateral plasma membrane; IEA:Compara.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0043005; C:neuron projection; IEA:Compara.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0030529; C:ribonucleoprotein complex; IEA:Compara.
 GO:0036057; C:slit diaphragm; ISS:UniProtKB.
 GO:0005509; F:calcium ion binding; TAS:BHF-UCL.
 GO:0005516; F:calmodulin binding; TAS:ProtInc.
 GO:0005096; F:GTPase activator activity; TAS:ProtInc.
 GO:0005095; F:GTPase inhibitor activity; TAS:ProtInc.
 GO:0005099; F:Ras GTPase activator activity; IEA:InterPro.
 GO:0071277; P:cellular response to calcium ion; IDA:BHF-UCL.
 GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
 GO:0072015; P:glomerular visceral epithelial cell development; ISS:UniProtKB.
 GO:0035305; P:negative regulation of dephosphorylation; IEA:Compara.
 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; IEA:Compara.
 GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
 GO:0007165; P:signal transduction; TAS:ProtInc.
 GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
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
 SM00456; WW 
PROSITE
 PS50021; CH
 PS50096; IQ
 PS00509; RAS_GTPASE_ACTIV_1
 PS50018; RAS_GTPASE_ACTIV_2
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2 
PRINTS