CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009275
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cell division control protein 42 homolog 
Protein Synonyms/Alias
 G25K GTP-binding protein 
Gene Name
 CDC42 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MQTIKCVVVGDGubiquitination[1]
107EITHHCPKTPFLLVGubiquitination[2, 3]
128DDPSTIEKLAKNKQKubiquitination[4]
133IEKLAKNKQKPITPEubiquitination[3, 4]
135KLAKNKQKPITPETAacetylation[5]
135KLAKNKQKPITPETAubiquitination[2, 3]
144ITPETAEKLARDLKAacetylation[5]
144ITPETAEKLARDLKAubiquitination[2, 3, 4]
153ARDLKAVKYVECSALubiquitination[2, 3]
163ECSALTQKGLKNVFDubiquitination[2, 3]
166ALTQKGLKNVFDEAIubiquitination[4]
183ALEPPEPKKSRRCVLubiquitination[2, 4, 6, 7]
184LEPPEPKKSRRCVLLubiquitination[2, 4, 7]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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] 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] 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]
 [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]
 [6] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [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
Functional Description
 Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Plays a role in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. Mediates CDC42-dependent cell migration. 
Sequence Annotation
 NP_BIND 10 17 GTP.
 NP_BIND 57 61 GTP (By similarity).
 NP_BIND 115 118 GTP.
 MOTIF 32 40 Effector region (Potential).
 MOD_RES 32 32 O-AMP-tyrosine; by Haemophilus IbpA.
 MOD_RES 35 35 O-AMP-threonine; by Vibrio VopS.
 MOD_RES 64 64 Phosphotyrosine; by SRC.
 MOD_RES 188 188 Cysteine methyl ester (By similarity).
 LIPID 188 188 S-geranylgeranyl cysteine (By  
Keyword
 3D-structure; Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Differentiation; Direct protein sequencing; GTP-binding; Lipoprotein; Membrane; Methylation; Neurogenesis; Nucleotide-binding; Phosphoprotein; Prenylation; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 191 AA 
Protein Sequence
MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP YTLGLFDTAG 60
QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE ITHHCPKTPF LLVGTQIDLR 120
DDPSTIEKLA KNKQKPITPE TAEKLARDLK AVKYVECSAL TQKGLKNVFD EAILAALEPP 180
EPKKSRRCVL L 191 
Gene Ontology
 GO:0045177; C:apical part of cell; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0030175; C:filopodium; IDA:UniProtKB.
 GO:0000139; C:Golgi membrane; ISS:BHF-UCL.
 GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0072686; C:mitotic spindle; IDA:UniProtKB.
 GO:0043005; C:neuron projection; IDA:BHF-UCL.
 GO:0043025; C:neuronal cell body; IDA:BHF-UCL.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0030141; C:secretory granule; IEA:Compara.
 GO:0051233; C:spindle midzone; IDA:UniProtKB.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; TAS:UniProtKB.
 GO:0019901; F:protein kinase binding; IDA:BHF-UCL.
 GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
 GO:0090135; P:actin filament branching; IEA:Compara.
 GO:0051017; P:actin filament bundle assembly; IEA:Compara.
 GO:0034332; P:adherens junction organization; IEA:Compara.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0060070; P:canonical Wnt receptor signaling pathway; IEA:Compara.
 GO:0003161; P:cardiac conduction system development; IEA:Compara.
 GO:0034613; P:cellular protein localization; IEA:Compara.
 GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
 GO:0090136; P:epithelial cell-cell adhesion; IEA:Compara.
 GO:0060684; P:epithelial-mesenchymal cell signaling; IEA:Compara.
 GO:0051683; P:establishment of Golgi localization; ISS:BHF-UCL.
 GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IEA:Compara.
 GO:0007163; P:establishment or maintenance of cell polarity; TAS:UniProtKB.
 GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
 GO:0046847; P:filopodium assembly; IEA:Compara.
 GO:0007030; P:Golgi organization; ISS:BHF-UCL.
 GO:0031069; P:hair follicle morphogenesis; IEA:Compara.
 GO:0060789; P:hair follicle placode formation; IEA:Compara.
 GO:0060047; P:heart contraction; IEA:Compara.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0031424; P:keratinization; IEA:Compara.
 GO:0003334; P:keratinocyte development; IEA:Compara.
 GO:0030225; P:macrophage differentiation; TAS:UniProtKB.
 GO:0035264; P:multicellular organism growth; IEA:Compara.
 GO:0042692; P:muscle cell differentiation; TAS:Reactome.
 GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
 GO:0010629; P:negative regulation of gene expression; IEA:Compara.
 GO:0031333; P:negative regulation of protein complex assembly; IPI:UniProtKB.
 GO:0048664; P:neuron fate determination; IEA:Compara.
 GO:0007097; P:nuclear migration; IEA:Compara.
 GO:0072384; P:organelle transport along microtubule; ISS:BHF-UCL.
 GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
 GO:0045740; P:positive regulation of DNA replication; IEA:Compara.
 GO:0010628; P:positive regulation of gene expression; IEA:Compara.
 GO:0071338; P:positive regulation of hair follicle cell proliferation; IEA:Compara.
 GO:0090316; P:positive regulation of intracellular protein transport; IEA:Compara.
 GO:0046330; P:positive regulation of JNK cascade; IEA:Compara.
 GO:0048554; P:positive regulation of metalloenzyme activity; IEA:Compara.
 GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
 GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Compara.
 GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Compara.
 GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Compara.
 GO:0031274; P:positive regulation of pseudopodium assembly; IDA:UniProtKB.
 GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
 GO:0051835; P:positive regulation of synapse structural plasticity; IEA:Compara.
 GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
 GO:0051489; P:regulation of filopodium assembly; IDA:UniProtKB.
 GO:0007088; P:regulation of mitosis; IEA:Compara.
 GO:0042176; P:regulation of protein catabolic process; IEA:Compara.
 GO:0043497; P:regulation of protein heterodimerization activity; IEA:Compara.
 GO:0045859; P:regulation of protein kinase activity; IEA:Compara.
 GO:0031647; P:regulation of protein stability; IEA:Compara.
 GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
 GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
 GO:0002040; P:sprouting angiogenesis; IEA:Compara.
 GO:0060661; P:submandibular salivary gland formation; IEA:Compara.
 GO:0031295; P:T cell costimulation; TAS:Reactome. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR001806; Small_GTPase.
 IPR003578; Small_GTPase_Rho. 
Pfam
 PF00071; Ras 
SMART
 SM00174; RHO 
PROSITE
 PS51420; RHO 
PRINTS
 PR00449; RASTRNSFRMNG.