CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-043071
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
115DNNSKWVKHWVKGGYubiquitination[1]
239SHKDEVVKIQSLARMubiquitination[1, 2, 3, 4]
344DLNLMDIKIGLLVKNubiquitination[5]
350IKIGLLVKNKITLQDubiquitination[1]
352IGLLVKNKITLQDVVubiquitination[1]
364DVVSHSKKLTKKNKEubiquitination[1]
368HSKKLTKKNKEQLSDubiquitination[1]
370KKLTKKNKEQLSDMMubiquitination[1, 4, 6, 7]
381SDMMMINKQKGGLKAubiquitination[1, 2]
387NKQKGGLKALSKEKRubiquitination[1]
455YLLLRLFKTALQEEIubiquitination[6]
516DDKSLNIKTDPVDIYubiquitination[1, 2, 7]
539SQTGEASKLPYDVTPubiquitination[1, 5, 6]
572NMRAVTDKFLSAIVSubiquitination[2]
583AIVSSVDKIPYGMRFubiquitination[1, 2, 4]
593YGMRFIAKVLKDSLHubiquitination[2]
658RNLGSIAKMLQHAASubiquitination[2, 4]
817RTILLNTKRLIVDVIubiquitination[1, 4]
870PDKMKKSKSVKEDSNubiquitination[1, 7]
873MKKSKSVKEDSNLTLubiquitination[4, 5, 6, 7]
893KIQTGLKKLTELGTVubiquitination[1, 4, 6]
903ELGTVDPKNKYQELIubiquitination[1, 6, 7]
905GTVDPKNKYQELINDubiquitination[1, 2, 4, 7]
956GEQVDYYKSYIKTCLubiquitination[1, 2, 3, 5, 6, 7]
960DYYKSYIKTCLDNLAubiquitination[1]
990KSKKISLKYTAARLHacetylation[8, 9]
990KSKKISLKYTAARLHubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] 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]
 [7] 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]
 [8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [9] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1085 AA 
Protein Sequence
MSAADEVDGL GVARPHYGSV LDNERLTAEE MDERRRGIWQ SNKDTQEAQK FALGIFAINE 60
AVESGDVGKT LSALRSPDVG LYGVIPECGE TYHSDLAEAK KKKLAVGDNN SKWVKHWVKG 120
GYYYYHNLET QEGGWDEPPN FVQNSMQLSR EEIQSSISGV TAAYNREQLW LANEGLITRL 180
QARCRGYLVR QEFRSRMNFL KKQIPAITCI QSQWRGYKQK KAYQDRLAYL RSHKDEVVKI 240
QSLARMHQAR KRYRDRLQYF RDHINDIIKI QAFIRANKAR DDYKTLINAE DPPMVVVRKF 300
VHLLDQSDQD FQEELDLMKM REEVITLIRS NQQLENDLNL MDIKIGLLVK NKITLQDVVS 360
HSKKLTKKNK EQLSDMMMIN KQKGGLKALS KEKREKLEAY QHLFYLLQTN PTYLAKLIFQ 420
MPQNKSTKFM DSVIFTLYNY ASNQREEYLL LRLFKTALQE EIKSKVDQIQ EIVTGNPTVI 480
KMVVSFNRGA RGQNALRQIL APVVKEIMDD KSLNIKTDPV DIYKSWVNQM ESQTGEASKL 540
PYDVTPEQAL AHEEVKTRLD SSIRNMRAVT DKFLSAIVSS VDKIPYGMRF IAKVLKDSLH 600
EKFPDAGEDE LLKIIGNLLY YRYMNPAIVA PDAFDIIDLS AGGQLTTDQR RNLGSIAKML 660
QHAASNKMFL GDNAHLSIIN EYLSQSYQKF RRFFQTACDV PELQDKFNVD EYSDLVTLTK 720
PVIYISIGEI INTHTLLLDH QDAIAPEHND PIHELLDDLG EVPTIESLIG ESSGNLNDPN 780
KEALAKTEVS LTLTNKFDVP GDENAEMDAR TILLNTKRLI VDVIRFQPGE TLTEILETPA 840
TSEQEAEHQR AMQRRAIRDA KTPDKMKKSK SVKEDSNLTL QEKKEKIQTG LKKLTELGTV 900
DPKNKYQELI NDIARDIRNQ RRYRQRRKAE LVKLQQTYAA LNSKATFYGE QVDYYKSYIK 960
TCLDNLASKG KVSKKPREMK GKKSKKISLK YTAARLHEKG VLLEIEDLQV NQFKNVIFEI 1020
SPTEEVGDFE VKAKFMGVQM ETFMLHYQDL LQLQYEGVAV MKLFDRAKVN VNLLIFLLNK 1080
KFYGK 1085 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0005099; F:Ras GTPase activator activity; IEA:InterPro.
 GO:0032320; P:positive regulation of Ras GTPase activity; IEA:GOC.
 GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. 
Interpro
 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
 PF00612; IQ
 PF00616; RasGAP
 PF03836; RasGAP_C 
SMART
 SM00015; IQ
 SM00323; RasGAP
 SM00456; WW 
PROSITE
 PS50096; IQ
 PS00509; RAS_GTPASE_ACTIV_1
 PS50018; RAS_GTPASE_ACTIV_2
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2 
PRINTS