DOCK2_MOUSE - dbPTM
DOCK2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DOCK2_MOUSE
UniProt AC Q8C3J5
Protein Name Dedicator of cytokinesis protein 2
Gene Name Dock2
Organism Mus musculus (Mouse).
Sequence Length 1828
Subcellular Localization Endomembrane system
Peripheral membrane protein. Cytoplasm, cytoskeleton. Colocalizes with F-actin..
Protein 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..
Protein Sequence MAPWRKTDKERHGVAIYNFQGSEAQHLTLQIGDVVRIQETCGDWYRGYLIKHKLSQGIFPTSFIHLKEVTVEKRRNIENIIPAEIPLAQEVTTTLWEWGSIWKQLYVASKKERFLQVQSMMYDLMEWRSQLLSGTLPKDELKELKQKVTSKIDYGNKILELDLIVRDEDGNILDPDKTSVISLFHAHEEATYKITERIKEEMSKDQPDYGVYSRISSSPTHSLYVFVRNFVCRIGEDAELFMSLYDPHKQTVISENYLVRWGSKGFPKEIEMLNNLKVVFTDLGNKDLNRDKIFLICQIVRIGKMDLKDINAKKCTQGLRRPFGVAVMDITDIIKGKAESDEEKQHFIPFHPVSAENDFLHSLLGKVIASKGDSGGQGLWVTMKMLVGDIIQIRKDYPHLVDRTTVVARKLGFPEIIMPGDVRNDIYITLLQGDFDKYTKTTQRNVEVIMCVCTEDGKVLPNAICVGAGDKAMNEYHSVVYYQVKQPRWMETVKVAVPIEDMQRIHLRFMFRHRSSLESKDKGEKNFAMSYVKLMKEDGTTLHDGYHELVVLKGDSKKMEDASAYLTLPSYRHPVENKGATLSRSSSSVGGLSVSSRDVFSISTLVCSTKLTQNVGLLGLLKWRMKPQLLQENLEKLKIVDGEEVVKFLQDTLDALFNIMMEHSQSNEYDILVFDALIYIIGLIADRKFQHFNTVLEAYIQQHFSATLAYKKLMTVLKTYLDTSSRGEQCEPILRTLKALEYVFKFIVRSRTLFSQLYEGKEQMEFEESMRRLFESINNLMKSQYKTTILLQVAALKYIPSVLHDVETVFDAKLLSQLLYEFYTCIPPVKLQKQKVQSMNEIVQSNLFKKQECRDILLPVITKELKELLEQRDDGQHQAEKKHCVELLNSILEVLSCQDAAFTYDHIQEIMVQLLRTVNRTVITMGRDHALISHFVACMTAILDQMGDQHYSFYIETFQTSSDLVDFLMETFIMFKDLIGKNVYPGDWMAMSMVQNRVFLRAINKFAETMNQKFLEHTSFEFQLWNNYFHLAVAFITQDSLQLEQFTHAKYNKILNKYGDMRRLIGFSIRDMWYKLGQNKICFIPGMVGPILEMTLIPEAELRKATIPIFFDMMLCEYQRTGAFKKFENEIILKLDHEVEGGRGDEQYMQLLESILMECTAEHPTIAKSVENFVSLVKGLLEKLLDYRGVMTDESKDNRMSCTVNLLNFYKDNNREEMYIRYLYKLRDLHLDCENYTEAAYTLLLHTWLLKWSDEQCASQVMQTGQQHPQTHRQLKETLYETIIGYFDKGKMWEEAISLCKELAEQYEMEIFDYELLSQNLTQQAKFYENIMKILRTKPDYFAVGYYGQGFPSFLRNKVFIYRGKEYERREDFQMQLLSQFPNAEKMNTTSAPGDDVRNAPGQYIQCFTVQPVLDEHPRFKNKPVPDQIINFYKSNYVQKFHYSRPVRRGKVDPENEFASMWIERTSFLTAYKLPGILRWFEVVHMSQTTISPLENAIETMSTVNEKILMMINQYQSDESLPINPLSMLLNGIVDPAVMGGFAKYEKAFFTEEYSREHPEDQDKLSHLKDLIAWQIPFLGAGIKIHEKRVSDNLRPFHDRMEECFKNLKMKVEKEYGVREMPDFEDRRVGRPRSMLRSYRQMSVISLASMHSDCSTPSKVPAESFDLESAPPKTPKVEEEPISPGSTLPEVKLRRSKKRTKRSSVVFADEKAATESDLKRLSRKQEFMSDTNLSEHAAIPARVSILSQMSFASQSMPTIPALTLSVAGVPGLDEANTSPRLSQTFFQVSDGDKKTLKKKKVNQFFKTMLASKSSEESKQIPDFLSTNM
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
7Phosphorylation-MAPWRKTDKERHGV
-CCCCCCCCHHHCEE		43.6720469934
151UbiquitinationLKQKVTSKIDYGNKI
HHHHHHHHCCCCCCE		30.17-
192PhosphorylationHAHEEATYKITERIK
ECCHHHHHHHHHHHH		13.87-
209PhosphorylationMSKDQPDYGVYSRIS
HCCCCCCCCCCCCCC		18.3825367039
212PhosphorylationDQPDYGVYSRISSSP
CCCCCCCCCCCCCCC		6.4620438120
213PhosphorylationQPDYGVYSRISSSPT
CCCCCCCCCCCCCCC		22.2622345495
304AcetylationCQIVRIGKMDLKDIN
EEHHEECCCCHHHCC		27.20-
354PhosphorylationFIPFHPVSAENDFLH
CCCCCCCCCCCHHHH		34.0225159016
362PhosphorylationAENDFLHSLLGKVIA
CCCHHHHHHHHHHHH		27.6925159016
397PhosphorylationIIQIRKDYPHLVDRT
HHHHHCCCCCCCCCC		8.7924719451
405PhosphorylationPHLVDRTTVVARKLG
CCCCCCCHHHHHHHC		17.5524719451
516PhosphorylationFMFRHRSSLESKDKG
HHHHCCCCCCCCCCC		35.7924719451
563PhosphorylationSKKMEDASAYLTLPS
CCCCCCCHHHEECCC		29.75-
585PhosphorylationKGATLSRSSSSVGGL
CCCEECCCCCCCCCC		31.0628833060
586PhosphorylationGATLSRSSSSVGGLS
CCEECCCCCCCCCCC		26.0628833060
587PhosphorylationATLSRSSSSVGGLSV
CEECCCCCCCCCCCC		30.2322942356
588PhosphorylationTLSRSSSSVGGLSVS
EECCCCCCCCCCCCC		27.0821082442
593PhosphorylationSSSVGGLSVSSRDVF
CCCCCCCCCCCCCCE		24.1924759943
595PhosphorylationSVGGLSVSSRDVFSI
CCCCCCCCCCCCEEE		19.1128833060
596PhosphorylationVGGLSVSSRDVFSIS
CCCCCCCCCCCEEEE		30.2828833060
608PhosphorylationSISTLVCSTKLTQNV
EEEHHHHCCCCCCCC		22.5429899451
714SulfoxidationTLAYKKLMTVLKTYL
HHHHHHHHHHHHHHH		3.1521406390
715PhosphorylationLAYKKLMTVLKTYLD
HHHHHHHHHHHHHHC		32.8725293948
719PhosphorylationKLMTVLKTYLDTSSR
HHHHHHHHHHCCCCC		25.7525293948
720PhosphorylationLMTVLKTYLDTSSRG
HHHHHHHHHCCCCCC		10.8625293948
723PhosphorylationVLKTYLDTSSRGEQC
HHHHHHCCCCCCCCC		26.4625293948
724PhosphorylationLKTYLDTSSRGEQCE
HHHHHCCCCCCCCCH		20.0825293948
725PhosphorylationKTYLDTSSRGEQCEP
HHHHCCCCCCCCCHH		46.5325293948
738AcetylationEPILRTLKALEYVFK
HHHHHHHHHHHHHHH		50.76-
755PhosphorylationVRSRTLFSQLYEGKE
HHHHHHHHHHHCCHH		23.5324719451
758PhosphorylationRTLFSQLYEGKEQME
HHHHHHHHCCHHHHH		18.2624719451
863UbiquitinationILLPVITKELKELLE
CHHHHHHHHHHHHHH		50.3422790023
933PhosphorylationGRDHALISHFVACMT
CCCHHHHHHHHHHHH		16.24-
940PhosphorylationSHFVACMTAILDQMG
HHHHHHHHHHHHHHC		15.49-
1058PhosphorylationYNKILNKYGDMRRLI
HHHHHHHHCHHHHHH		19.79-
1187PhosphorylationLLEKLLDYRGVMTDE
HHHHHHHHCCCCCCC		14.83-
1379PhosphorylationDFQMQLLSQFPNAEK
HHHHHHHHCCCCHHH		38.0730635358
1591PhosphorylationKIHEKRVSDNLRPFH
EEEEHHHHCCCCCCH		25.4724704852
1634PhosphorylationRRVGRPRSMLRSYRQ
CCCCCCHHHHHHHHH		25.5025266776
1638PhosphorylationRPRSMLRSYRQMSVI
CCHHHHHHHHHHHHH		22.2427600695
1643PhosphorylationLRSYRQMSVISLASM
HHHHHHHHHHHHHHC		14.1425266776
1646PhosphorylationYRQMSVISLASMHSD
HHHHHHHHHHHCCCC		18.7425266776
1664PhosphorylationPSKVPAESFDLESAP
CCCCCHHHCCCCCCC		26.6027180971
1669PhosphorylationAESFDLESAPPKTPK
HHHCCCCCCCCCCCC		54.0629472430
1674PhosphorylationLESAPPKTPKVEEEP
CCCCCCCCCCCCCCC		33.8328725479
1683PhosphorylationKVEEEPISPGSTLPE
CCCCCCCCCCCCCCH		33.6425521595
1686PhosphorylationEEPISPGSTLPEVKL
CCCCCCCCCCCHHHC		30.1028833060
1687PhosphorylationEPISPGSTLPEVKLR
CCCCCCCCCCHHHCC		52.8522942356
1700PhosphorylationLRRSKKRTKRSSVVF
CCCCCCCCCCCCEEE		39.4228285833
1703PhosphorylationSKKRTKRSSVVFADE
CCCCCCCCCEEECCH		29.1023375375
1704PhosphorylationKKRTKRSSVVFADEK
CCCCCCCCEEECCHH		26.7425521595
1714PhosphorylationFADEKAATESDLKRL
ECCHHHCCHHHHHHH		40.6622345495
1716PhosphorylationDEKAATESDLKRLSR
CHHHCCHHHHHHHHH		43.8422345495
1722PhosphorylationESDLKRLSRKQEFMS
HHHHHHHHHHHHHHC		41.2724719451
1729PhosphorylationSRKQEFMSDTNLSEH
HHHHHHHCCCCHHHH		46.7526824392
1731PhosphorylationKQEFMSDTNLSEHAA
HHHHHCCCCHHHHCC		30.6522942356
1734PhosphorylationFMSDTNLSEHAAIPA
HHCCCCHHHHCCHHH		29.4328833060
1753PhosphorylationLSQMSFASQSMPTIP
HHHCCHHCCCCCCCC		22.3027600695
1755PhosphorylationQMSFASQSMPTIPAL
HCCHHCCCCCCCCEE		25.0027600695
1765PhosphorylationTIPALTLSVAGVPGL
CCCEEEEEECCCCCC		12.5127600695
1777PhosphorylationPGLDEANTSPRLSQT
CCCCCCCCCCCHHHE		47.3528576409
1778PhosphorylationGLDEANTSPRLSQTF
CCCCCCCCCCHHHEE		14.0828576409
1782PhosphorylationANTSPRLSQTFFQVS
CCCCCCHHHEEEECC		28.5827566939
1784PhosphorylationTSPRLSQTFFQVSDG
CCCCHHHEEEECCCC		24.0428833060
1789PhosphorylationSQTFFQVSDGDKKTL
HHEEEECCCCCHHHH		25.7019854140
1807PhosphorylationKVNQFFKTMLASKSS
HHHHHHHHHHHCCCH		16.5624719451
1811PhosphorylationFFKTMLASKSSEESK
HHHHHHHCCCHHHHH		29.1630635358
1813PhosphorylationKTMLASKSSEESKQI
HHHHHCCCHHHHHCC		40.2527600695
1814PhosphorylationTMLASKSSEESKQIP
HHHHCCCHHHHHCCC		49.4727600695
1817PhosphorylationASKSSEESKQIPDFL
HCCCHHHHHCCCCHH		26.3030635358
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of DOCK2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DOCK2_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DOCK2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DOCK2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DOCK2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1704, AND MASSSPECTROMETRY.

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