CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018769
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dedicator of cytokinesis protein 2 
Protein Synonyms/Alias
  
Gene Name
 DOCK2 
Gene Synonyms/Alias
 KIAA0209 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
51WYRGYLIKHKMLQGIubiquitination[1]
61MLQGIFPKSFIHIKEubiquitination[2]
67PKSFIHIKEVTVEKRacetylation[3]
67PKSFIHIKEVTVEKRubiquitination[1]
110KQLYVASKKERFLQVubiquitination[1]
111QLYVASKKERFLQVQubiquitination[1]
138LLSGTLPKDELKELKubiquitination[1]
145KDELKELKQKVTSKIubiquitination[1]
151LKQKVTSKIDYGNKIubiquitination[1]
199DKITERIKEEMSKDQubiquitination[1, 4]
204RIKEEMSKDQPDYAMubiquitination[1]
268WGSRGFPKEIEMLNNubiquitination[1, 2]
286VFTDLGNKDLNRDKIubiquitination[1]
304CQIVRVGKMDLKDTGacetylation[3]
304CQIVRVGKMDLKDTGubiquitination[1]
308RVGKMDLKDTGAKKCubiquitination[1]
335MDITDIIKGKAESDEubiquitination[1]
337ITDIIKGKAESDEEKubiquitination[1]
371LGKVIASKGDSGGQGubiquitination[1, 2, 4]
395GDIIQIRKDYPHLVDubiquitination[1]
410RTTVVARKLGFPEIIubiquitination[1, 2]
437LLQGDFDKYNKTTQRubiquitination[1]
440GDFDKYNKTTQRNVEubiquitination[1]
471ICVGAGDKPMNEYRSubiquitination[1]
485SVVYYQVKQPRWMETubiquitination[1]
494PRWMETVKVAVPIEDubiquitination[1, 4]
525ESKDKGEKNFAMSYVubiquitination[1]
533NFAMSYVKLMKEDGTubiquitination[1]
558VLKGDSKKMEDASAYubiquitination[1]
578YRHHVENKGATLSRSubiquitination[1, 5]
610STLVCSTKLTQNVGLubiquitination[5]
622VGLLGLLKWRMKPQLubiquitination[1, 2, 4, 5]
626GLLKWRMKPQLLQENubiquitination[1]
738EPILRTLKALEYVFKacetylation[3]
835PVKLQKQKVQSMNEIubiquitination[1]
849IVQSNLFKKQECRDIubiquitination[1]
850VQSNLFKKQECRDILubiquitination[1]
863ILLPVITKELKELLEubiquitination[1, 2]
866PVITKELKELLEQKDubiquitination[1]
872LKELLEQKDDMQHQVubiquitination[1]
1006VFLRAINKFAETMNQubiquitination[1]
1054FSHAKYNKILNKYGDubiquitination[1, 5]
1058KYNKILNKYGDMRRLubiquitination[1]
1076SIRDMWYKLGQNKICubiquitination[1, 2]
1127QRSGDFKKFENEIILubiquitination[1, 2]
1179ENFVNLVKGLLEKLLubiquitination[1]
1184LVKGLLEKLLDYRGVubiquitination[1, 2]
1226MYIRYLYKLRDLHLDubiquitination[1]
1359FPSFLRNKVFIYRGKubiquitination[1]
1399SAPGDDVKNAPGQYIubiquitination[1]
1422LDEHPRFKNKPVPDQubiquitination[1]
1424EHPRFKNKPVPDQIIubiquitination[1, 2]
1435DQIINFYKSNYVQRFubiquitination[1, 2]
1474TSFVTAYKLPGILRWubiquitination[1, 2]
1548GGFAKYEKAFFTEEYubiquitination[1]
1607DRMEECFKNLKMKVEubiquitination[1]
1610EECFKNLKMKVEKEYubiquitination[1]
1612CFKNLKMKVEKEYGVubiquitination[1]
1615NLKMKVEKEYGVREMubiquitination[1]
1694GSTLPEVKLRRSKKRubiquitination[1]
1713SVVFADEKAAAESDLubiquitination[1]
1726DLKRLSRKHEFMSDTubiquitination[1]
1795LQLSDGDKKTLTRKKubiquitination[1]
1796QLSDGDKKTLTRKKVubiquitination[1]
1801DKKTLTRKKVNQFFKubiquitination[1]
1802KKTLTRKKVNQFFKTubiquitination[1]
1808KKVNQFFKTMLASKSubiquitination[2]
1814FKTMLASKSAEEGKQubiquitination[1]
1820SKSAEEGKQIPDSLSubiquitination[1, 4]
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] 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]
 [4] 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]
 [5] 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
 Involved in cytoskeletal rearrangements required for lymphocyte migration in response of chemokines. Activates RAC1 and RAC2, but not CDC42, by functioning as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. May also participate in IL2 transcriptional activation via the activation of RAC2. 
Sequence Annotation
 DOMAIN 8 69 SH3.
 DOMAIN 423 607 DHR-1.
 DOMAIN 1211 1622 DHR-2.
 REGION 939 1476 Interaction with CRKL.
 MOD_RES 304 304 N6-acetyllysine.
 MOD_RES 588 588 Phosphoserine.
 MOD_RES 593 593 Phosphoserine.
 MOD_RES 738 738 N6-acetyllysine.
 MOD_RES 1685 1685 Phosphoserine.
 MOD_RES 1706 1706 Phosphoserine (By similarity).
 MOD_RES 1731 1731 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Guanine-nucleotide releasing factor; Membrane; Phosphoprotein; Polymorphism; Reference proteome; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1830 AA 
Protein Sequence
MAPWRKADKE RHGVAIYNFQ GSGAPQLSLQ IGDVVRIQET CGDWYRGYLI KHKMLQGIFP 60
KSFIHIKEVT VEKRRNTENI IPAEIPLAQE VTTTLWEWGS IWKQLYVASK KERFLQVQSM 120
MYDLMEWRSQ LLSGTLPKDE LKELKQKVTS KIDYGNKILE LDLIVRDEDG NILDPDNTSV 180
ISLFHAHEEA TDKITERIKE EMSKDQPDYA MYSRISSSPT HSLYVFVRNF VCRIGEDAEL 240
FMSLYDPNKQ TVISENYLVR WGSRGFPKEI EMLNNLKVVF TDLGNKDLNR DKIYLICQIV 300
RVGKMDLKDT GAKKCTQGLR RPFGVAVMDI TDIIKGKAES DEEKQHFIPF HPVTAENDFL 360
HSLLGKVIAS KGDSGGQGLW VTMKMLVGDI IQIRKDYPHL VDRTTVVARK LGFPEIIMPG 420
DVRNDIYITL LQGDFDKYNK TTQRNVEVIM CVCAEDGKTL PNAICVGAGD KPMNEYRSVV 480
YYQVKQPRWM ETVKVAVPIE DMQRIHLRFM FRHRSSLESK DKGEKNFAMS YVKLMKEDGT 540
TLHDGFHDLV VLKGDSKKME DASAYLTLPS YRHHVENKGA TLSRSSSSVG GLSVSSRDVF 600
SISTLVCSTK LTQNVGLLGL LKWRMKPQLL QENLEKLKIV DGEEVVKFLQ DTLDALFNIM 660
MEHSQSDEYD ILVFDALIYI IGLIADRKFQ HFNTVLEAYI QQHFSATLAY KKLMTVLKTY 720
LDTSSRGEQC EPILRTLKAL EYVFKFIVRS RTLFSQLYEG KEQMEFEESM RRLFESINNL 780
MKSQYKTTIL LQVAALKYIP SVLHDVEMVF DAKLLSQLLY EFYTCIPPVK LQKQKVQSMN 840
EIVQSNLFKK QECRDILLPV ITKELKELLE QKDDMQHQVL ERKYCVELLN SILEVLSYQD 900
AAFTYHHIQE IMVQLLRTVN RTVITMGRDH ILISHFVACM TAILNQMGDQ HYSFYIETFQ 960
TSSELVDFLM ETFIMFKDLI GKNVYPGDWM AMSMVQNRVF LRAINKFAET MNQKFLEHTN 1020
FEFQLWNNYF HLAVAFITQD SLQLEQFSHA KYNKILNKYG DMRRLIGFSI RDMWYKLGQN 1080
KICFIPGMVG PILEMTLIPE AELRKATIPI FFDMMLCEYQ RSGDFKKFEN EIILKLDHEV 1140
EGGRGDEQYM QLLESILMEC AAEHPTIAKS VENFVNLVKG LLEKLLDYRG VMTDESKDNR 1200
MSCTVNLLNF YKDNNREEMY IRYLYKLRDL HLDCDNYTEA AYTLLLHTWL LKWSDEQCAS 1260
QVMQTGQQHP QTHRQLKETL YETIIGYFDK GKMWEEAISL CKELAEQYEM EIFDYELLSQ 1320
NLIQQAKFYE SIMKILRPKP DYFAVGYYGQ GFPSFLRNKV FIYRGKEYER REDFQMQLMT 1380
QFPNAEKMNT TSAPGDDVKN APGQYIQCFT VQPVLDEHPR FKNKPVPDQI INFYKSNYVQ 1440
RFHYSRPVRR GTVDPENEFA SMWIERTSFV TAYKLPGILR WFEVVHMSQT TISPLENAIE 1500
TMSTANEKIL MMINQYQSDE TLPINPLSML LNGIVDPAVM GGFAKYEKAF FTEEYVRDHP 1560
EDQDKLTHLK DLIAWQIPFL GAGIKIHEKR VSDNLRPFHD RMEECFKNLK MKVEKEYGVR 1620
EMPDFDDRRV GRPRSMLRSY RQMSIISLAS MNSDCSTPSK PTSESFDLEL ASPKTPRVEQ 1680
EEPISPGSTL PEVKLRRSKK RTKRSSVVFA DEKAAAESDL KRLSRKHEFM SDTNLSEHAA 1740
IPLKASVLSQ MSFASQSMPT IPALALSVAG IPGLDEANTS PRLSQTFLQL SDGDKKTLTR 1800
KKVNQFFKTM LASKSAEEGK QIPDSLSTDL 1830 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IEA:UniProtKB-KW.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0020037; F:heme binding; IEA:InterPro.
 GO:0030675; F:Rac GTPase activator activity; IEA:Compara.
 GO:0030676; F:Rac guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
 GO:0042608; F:T cell receptor binding; IDA:UniProtKB.
 GO:0030036; P:actin cytoskeleton organization; TAS:UniProtKB.
 GO:0046633; P:alpha-beta T cell proliferation; IEA:Compara.
 GO:0006935; P:chemotaxis; IEA:Compara.
 GO:0001768; P:establishment of T cell polarity; IEA:Compara.
 GO:0001771; P:immunological synapse formation; IEA:Compara.
 GO:0044351; P:macropinocytosis; ISS:UniProtKB.
 GO:0001766; P:membrane raft polarization; IEA:Compara.
 GO:0002277; P:myeloid dendritic cell activation involved in immune response; ISS:UniProtKB.
 GO:0045060; P:negative thymic T cell selection; IEA:Compara.
 GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
 GO:0045059; P:positive thymic T cell selection; IEA:Compara.
 GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
 GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
 GO:0016032; P:viral reproduction; TAS:Reactome. 
Interpro
 IPR009056; Cyt_c_dom.
 IPR027007; DHR-1_domain.
 IPR027357; DHR-2.
 IPR026791; DOCK.
 IPR026799; DOCK_A.
 IPR010703; DOCK_C.
 IPR011511; SH3_2.
 IPR001452; SH3_domain. 
Pfam
 PF06920; Ded_cyto
 PF14429; DOCK-C2
 PF07653; SH3_2 
SMART
 SM00326; SH3 
PROSITE
 PS51650; DHR_1
 PS51651; DHR_2
 PS50002; SH3 
PRINTS