CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001100
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SLIT-ROBO Rho GTPase-activating protein 2 
Protein Synonyms/Alias
 srGAP2; Formin-binding protein 2; Rho GTPase-activating protein 34 
Gene Name
 SRGAP2 
Gene Synonyms/Alias
 ARHGAP34; FNBP2; KIAA0456; SRGAP2A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
22AEYDTQVKEIRAQLTubiquitination[1]
33AQLTEQMKCLDQQCEubiquitination[1, 2]
88TKDQQFKKDQNVLSPubiquitination[1]
143GRLFKKSKEVGQQLQubiquitination[1]
180DSISAQSKLKEAEKQubiquitination[1]
306ELNLEQSKHEGLDAIubiquitination[3]
326NLDATSDKQRLMEMYubiquitination[3]
381QSRLSTLKIENEEVKubiquitination[1]
433VSETFMSKPSIAKRRubiquitination[3]
470LITKLQAKHDLLQKTubiquitination[1]
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] 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]
 [3] 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
 RAC1 GTPase activating protein (GAP) that binds and deforms membranes, and regulates actin dynamics to regulate cell migration and differentiation. Plays an important role in different aspects of neuronal morphogenesis and migration mainly during development of the cerebral cortex. This includes the biogenesis of neurites, where it is required for both axons and dendrites outgrowth, and the maturation of the dendritic spines. Also stimulates the branching of the leading process and negatively regulates neuron radial migration in the cerebral cortex. Its interaction and inhibition by SRGAP2C reduces the rate of spine maturation, alters dendritic spine morphology and density and indirectly increases neuronal migration. It may have implications for cognition, learning and memory. In non-neuronal cells, it may also play a role in cell migration by regulating the formation of lamellipodia and filopodia. 
Sequence Annotation
 DOMAIN 22 87 FCH.
 DOMAIN 489 679 Rho-GAP.
 DOMAIN 728 787 SH3.
 REGION 1 501 F-BAR domain.
 MOD_RES 799 799 Phosphoserine (By similarity).
 MOD_RES 927 927 Omega-N-methylated arginine; by PRMT5.
 MOD_RES 930 930 Phosphoserine.  
Keyword
 3D-structure; Cell junction; Cell membrane; Cell projection; Chromosomal rearrangement; Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle; GTPase activation; Membrane; Methylation; Neurogenesis; Nucleus; Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Reference proteome; SH3 domain; Synapse. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1071 AA 
Protein Sequence
MTSPAKFKKD KEIIAEYDTQ VKEIRAQLTE QMKCLDQQCE LRVQLLQDLQ DFFRKKAEIE 60
MDYSRNLEKL AERFLAKTRS TKDQQFKKDQ NVLSPVNCWN LLLNQVKRES RDHTTLSDIY 120
LNNIIPRFVQ VSEDSGRLFK KSKEVGQQLQ DDLMKVLNEL YSVMKTYHMY NADSISAQSK 180
LKEAEKQEEK QIGKSVKQED RQTPRSPDST ANVRIEEKHV RRSSVKKIEK MKEKRQAKYT 240
ENKLKAIKAR NEYLLALEAT NASVFKYYIH DLSDLIDQCC DLGYHASLNR ALRTFLSAEL 300
NLEQSKHEGL DAIENAVENL DATSDKQRLM EMYNNVFCPP MKFEFQPHMG DMASQLCAQQ 360
PVQSELVQRC QQLQSRLSTL KIENEEVKKT MEATLQTIQD IVTVEDFDVS DCFQYSNSME 420
SVKSTVSETF MSKPSIAKRR ANQQETEQFY FTKMKEYLEG RNLITKLQAK HDLLQKTLGE 480
SQRTDCSLAR RSSTVRKQDS SQAIPLVVES CIRFISRHGL QHEGIFRVSG SQVEVNDIKN 540
AFERGEDPLA GDQNDHDMDS IAGVLKLYFR GLEHPLFPKD IFHDLMACVT MDNLQERALH 600
IRKVLLVLPK TTLIIMRYLF AFLNHLSQFS EENMMDPYNL AICFGPSLMS VPEGHDQVSC 660
QAHVNELIKT IIIQHENIFP SPRELEGPVY SRGGSMEDYC DSPHGETTPV EDSTQDVTAE 720
HHTSDDECEP IEAIAKFDYV GRTARELSFK KGASLLLYQR ASDDWWEGRH NGIDGLIPHQ 780
YIVVQDTEDG VVERSSPKSE IEVISEPPEE KVTARAGASC PSGGHVADIY LANINKQRKR 840
PESGSIRKTF RSDSHGLSSS LTDSSSPGVG ASCRPSSQPI MSQSLPKEGP DKCSISGHGS 900
LNSISRHSSL KNRLDSPQIR KTATAGRSKS FNNHRPMDPE VIAQDIEATM NSALNELREL 960
ERQSSVKHTP DVVLDTLEPL KTSPVVAPTS EPSSPLHTQL LKDPEPAFQR SASTAGDIAC 1020
AFRPVKSVKM AAPVKPPATR PKPTVFPKTN ATSPGVNSST SPQSTDKSCT V 1071 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0030027; C:lamellipodium; IDA:UniProtKB.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0014069; C:postsynaptic density; ISS:UniProtKB.
 GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0030675; F:Rac GTPase activator activity; IDA:UniProtKB.
 GO:0048365; F:Rac GTPase binding; IDA:UniProtKB.
 GO:0051014; P:actin filament severing; IDA:UniProtKB.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0060996; P:dendritic spine development; IDA:UniProtKB.
 GO:0021816; P:extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration; ISS:UniProtKB.
 GO:0046847; P:filopodium assembly; IDA:UniProtKB.
 GO:0003363; P:lamellipodium assembly involved in ameboidal cell migration; IMP:UniProtKB.
 GO:2001223; P:negative regulation of neuron migration; IDA:UniProtKB.
 GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
 GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB. 
Interpro
 IPR001060; FCH_dom.
 IPR008936; Rho_GTPase_activation_prot.
 IPR000198; RhoGAP_dom.
 IPR001452; SH3_domain. 
Pfam
 PF00611; FCH
 PF00620; RhoGAP
 PF00018; SH3_1 
SMART
 SM00055; FCH
 SM00324; RhoGAP
 SM00326; SH3 
PROSITE
 PS50133; FCH
 PS50238; RHOGAP
 PS50002; SH3 
PRINTS