CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012155
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ras GTPase-activating-like protein IQGAP2 
Protein Synonyms/Alias
  
Gene Name
 IQGAP2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
171QIQDLLGKVDFTEEEubiquitination[1]
590LVKAKELKSERVSSDubiquitination[2, 3]
631TPESCLYKESWLTGKubiquitination[3]
756DHNNEIVKIQSLLRAubiquitination[3]
814LREEVVTKIRANQQLubiquitination[3]
837IKIGLLVKNRITLEDubiquitination[3]
856SKKLNKKKGGEMEILubiquitination[3]
1467RSIKLDGKGEPKGAKacetylation[4]
1471LDGKGEPKGAKRAKPacetylation[4, 5]
1474KGEPKGAKRAKPVKYacetylation[5]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861
Functional Description
 Binds to activated CDC42 and RAC1 but does not seem to stimulate their GTPase activity. Associates with calmodulin. 
Sequence Annotation
 DOMAIN 41 156 CH.
 DOMAIN 594 627 WW.
 DOMAIN 690 719 IQ 1.
 DOMAIN 720 749 IQ 2.
 DOMAIN 750 779 IQ 3.
 DOMAIN 917 1150 Ras-GAP.
 MOD_RES 16 16 Phosphoserine.
 MOD_RES 1389 1389 Phosphoserine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Calmodulin-binding; Complete proteome; Direct protein sequencing; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1575 AA 
Protein Sequence
MPHEELPSLQ RPRYGSIVDD ERLSAEEMDE RRRQNIAYEY LCHLEEAKRW MEVCLVEELP 60
PTTELEEGLR NGVYLAKLAK FFAPKMVSEK KIYDVEQTRY KKSGLHFRHT DNTVQWLRAM 120
ESIGLPKIFY PETTDVYDRK NIPRMIYCIH ALSLYLFKLG IAPQIQDLLG KVDFTEEEIS 180
NMRKELEKYG IQMPSFSKIG GILANELSVD EAALHAAVIA INEAVEKGIA EQTVVTLRNP 240
NAVLTLVDDN LAPEYQKELW DAKKKKEENA RLKNSCISEE ERDAYEELLT QAEIQGNINK 300
VNRQAAVDHI NAVIPEGDPE NTLLALKKPE AQLPAVYPFA AAMYQNELFN LQKQNTMNYL 360
AHEELLIAVE MLSAVALLNQ ALESNDLVSV QNQLRSPAIG LNNLDKAYVE RYANTLLSVK 420
LEVLSQGQDN LSWNEIQNCI DMVNAQIQEE NDRVVAVGYI NEAIDEGNPL RTLETLLLPT 480
ANISDVDPAH AQHYQDVLYH AKSQKLGDSE SVSKVLWLDE IQQAVDDANV DKDRAKQWVT 540
LVVDVNQCLE GKKSSDILSV LKSSTSNAND IIPECADKYY DALVKAKELK SERVSSDGSW 600
LKLNLHKKYD YYYNTDSKES SWVTPESCLY KESWLTGKEI EDIIEEVTVG YIRENIWSAS 660
EELLLRFQAT SSGPILREEF EARKSFLHEQ EENVVKIQAF WKGYKQRKEY MHRRQTFIDN 720
TDSIVKIQSW FRMATARKSY LSRLQYFRDH NNEIVKIQSL LRANKARDDY KTLVGSENPP 780
LTVIRKFVYL LDQSDLDFQE ELEVARLREE VVTKIRANQQ LEKDLNLMDI KIGLLVKNRI 840
TLEDVISHSK KLNKKKGGEM EILNNTDNQG IKSLSKERRK TLETYQQLFY LLQTNPLYLA 900
KLIFQMPQNK STKFMDTVIF TLYNYASNQR EEYLLLKLFK TALEEEIKSK VDQVQDIVTG 960
NPTVIKMVVS FNRGARGQNT LRQLLAPVVK EIIDDKSLII NTNPVEVYKA WVNQLETQTG 1020
EASKLPYDVT TEQALTYPEV KNKLEASIEN LRRVTDKVLN SIISSLDLLP YGLRYIAKVL 1080
KNSIHEKFPD ATEDELLKIV GNLLYYRYMN PAIVAPDGFD IIDMTAGGQI NSDQRRNLGS 1140
VAKVLQHAAS NKLFEGENEH LSSMNNYLSE TYQEFRKYFK EACNVPEPEE KFNMDKYTDL 1200
VTVSKPVIYI SIEEIISTHS LLLEHQDAIA PEKNDLLSEL LGSLGEVPTV ESFLGEGAVD 1260
PNDPNKANTL SQLSKTEISL VLTSKYDIED GEAIDSRSLM IKTKKLIIDV IRNQPGNTLT 1320
EILETPATAQ QEVDHATDMV SRAMIDSRTP EEMKHSQSMI EDAQLPLEQK KRKIQRNLRT 1380
LEQTGHVSSE NKYQDILNEI AKDIRNQRIY RKLRKAELAK LQQTLNALNK KAAFYEEQIN 1440
YYDTYIKTCL DNLKRKNTRR SIKLDGKGEP KGAKRAKPVK YTAAKLHEKG VLLDIDDLQT 1500
NQFKNVTFDI IATEDVGIFD VRSKFLGVEM EKVQLNIQDL LQMQYEGVAV MKMFDKVKVN 1560
VNLLIYLLNK KFYGK 1575 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0005902; C:microvillus; IEA:Compara.
 GO:0003779; F:actin binding; TAS:ProtInc.
 GO:0005095; F:GTPase inhibitor activity; TAS:ProtInc.
 GO:0005099; F:Ras GTPase activator activity; IEA:InterPro.
 GO:0032320; P:positive regulation of Ras GTPase activity; IEA:GOC.
 GO:0007165; P:signal transduction; TAS:ProtInc.
 GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. 
Interpro
 IPR001715; CH-domain.
 IPR000048; IQ_motif_EF-hand-BS.
 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