DOCK4_HUMAN - dbPTM
DOCK4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DOCK4_HUMAN
UniProt AC Q8N1I0
Protein Name Dedicator of cytokinesis protein 4
Gene Name DOCK4
Organism Homo sapiens (Human).
Sequence Length 1966
Subcellular Localization Cell membrane . Cell projection . Cytoplasm, cytosol . Colocalizes with EPHA2, RhoG and CTTN/cortactin at the tip of protrusions in migrating cells.
Protein Description Involved in regulation of adherens junction between cells. Plays a role in cell migration. Functions as a guanine nucleotide exchange factor (GEF), which activates Rap1 small GTPase by exchanging bound GDP for free GTP..
Protein Sequence MWIPTEHEKYGVVIASFRGTVPYGLSLEIGDTVQILEKCDGWYRGFALKNPNIKGIFPSSYVHLKNACVKNKGQFEMVIPTEDSVITEMTSTLRDWGTMWKQLYVRNEGDLFHRLWHIMNEILDLRRQVLVGHLTHDRMKDVKRHITARLDWGNEQLGLDLVPRKEYAMVDPEDISITELYRLMEHRHRKKDTPVQASSHHLFVQMKSLMCSNLGEELEVIFSLFDSKENRPISERFFLRLNRNGLPKAPDKPERHCSLFVDLGSSELRKDIYITVHIIRIGRMGAGEKKNACSVQYRRPFGCAVLSIADLLTGETKDDLILKVYMCNTESEWYQIHENIIKKLNARYNLTGSNAGLAVSLQLLHGDIEQIRREYSSVFSHGVSITRKLGFSNIIMPGEMRNDLYITIERGEFEKGGKSVARNVEVTMFIVDSSGQTLKDFISFGSGEPPASEYHSFVLYHNNSPRWSELLKLPIPVDKFRGAHIRFEFRHCSTKEKGEKKLFGFSFVPLMQEDGRTLPDGTHELIVHKCEENTNLQDTTRYLKLPFSKGIFLGNNNQAMKATKESFCITSFLCSTKLTQNGDMLDLLKWRTHPDKITGCLSKLKEIDGSEIVKFLQDTLDTLFGILDENSQKYGSKVFDSLVHIINLLQDSKFHHFKPVMDTYIESHFAGALAYRDLIKVLKWYVDRITEAERQEHIQEVLKAQEYIFKYIVQSRRLFSLATGGQNEEEFRCCIQELLMSVRFFLSQESKGSGALSQSQAVFLSSFPAVYSELLKLFDVREVANLVQDTLGSLPTILHVDDSLQAIKLQCIGKTVESQLYTNPDSRYILLPVVLHHLHIHLQEQKDLIMCARILSNVFCLIKKNSSEKSVLEEIDVIVASLLDILLRTILEITSRPQPSSSAMRFQFQDVTGEFVACLLSLLRQMTDRHYQQLLDSFNTKEELRDFLLQIFTVFRILIRPEMFPKDWTVMRLVANNVIITTVLYLSDALRKNFLNENFDYKIWDSYFYLAVIFINQLCLQLEMFTPSKKKKVLEKYGDMRVTMGCEIFSMWQNLGEHKLHFIPALIGPFLEVTLIPQPDLRNVMIPIFHDMMDWEQRRSGNFKQVEAKLIDKLDSLMSEGKGDETYRELFNSILLKKIERETWRESGVSLIATVTRLMERLLDYRDCMKMGEVDGKKIGCTVSLLNFYKTELNKEEMYIRYIHKLYDLHLKAQNFTEAAYTLLLYDELLEWSDRPLREFLTYPMQTEWQRKEHLHLTIIQNFDRGKCWENGIILCRKIAEQYESYYDYRNLSKMRMMEASLYDKIMDQQRLEPEFFRVGFYGKKFPFFLRNKEFVCRGHDYERLEAFQQRMLNEFPHAIAMQHANQPDETIFQAEAQYLQIYAVTPIPESQEVLQREGVPDNIKSFYKVNHIWKFRYDRPFHKGTKDKENEFKSLWVERTSLYLVQSLPGISRWFEVEKREVVEMSPLENAIEVLENKNQQLKTLISQCQTRQMQNINPLTMCLNGVIDAAVNGGVSRYQEAFFVKEYILSHPEDGEKIARLRELMLEQAQILEFGLAVHEKFVPQDMRPLHKKLVDQFFVMKSSLGIQEFSACMQASPVHFPNGSPRVCRNSAPASVSPDGTRVIPRRSPLSYPAVNRYSSSSLSSQASAEVSNITGQSESSDEVFNMQPSPSTSSLSSTHSASPNVTSSAPSSARASPLLSDKHKHSRENSCLSPRERPCSAIYPTPVEPSQRMLFNHIGDGALPRSDPNLSAPEKAVNPTPSSWSLDSGKEAKNMSDSGKLISPPVPPRPTQTASPARHTTSVSPSPAGRSPLKGSVQSFTPSPVEYHSPGLISNSPVLSGSYSSGISSLSRCSTSETSGFENQVNEQSAPLPVPVPVPVPSYGGEEPVRKESKTPPPYSVYERTLRRPVPLPHSLSIPVTSEPPALPPKPLAARSSHLENGARRTDPGPRPRPLPRKVSQL
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
20PhosphorylationVIASFRGTVPYGLSL
EEEEECCCCCCCEEE		17.6623898821
23PhosphorylationSFRGTVPYGLSLEIG
EECCCCCCCEEEEEC		26.7723898821
26PhosphorylationGTVPYGLSLEIGDTV
CCCCCCEEEEECCHH		21.4223898821
32PhosphorylationLSLEIGDTVQILEKC
EEEEECCHHHHHHHC		14.7523898821
101UbiquitinationRDWGTMWKQLYVRNE
HHHHHHHHHHHCCCC		21.4321890473
101 (in isoform 1)Ubiquitination-21.4321890473
101 (in isoform 2)Ubiquitination-21.4321890473
101 (in isoform 3)Ubiquitination-21.4321890473
112UbiquitinationVRNEGDLFHRLWHIM
CCCCCHHHHHHHHHH		3.6121890473
132UbiquitinationLRRQVLVGHLTHDRM
HHHHHHHHCCCHHHH		13.1121890473
167PhosphorylationDLVPRKEYAMVDPED
CCCCCHHHCCCCHHH		11.7527196784
181PhosphorylationDISITELYRLMEHRH
HCCHHHHHHHHHHHC		8.75-
193PhosphorylationHRHRKKDTPVQASSH
HHCCCCCCCCCCCHH		33.9522210691
348PhosphorylationIKKLNARYNLTGSNA
HHHHHHHCCCCCCCH		16.4724719451
351PhosphorylationLNARYNLTGSNAGLA
HHHHCCCCCCCHHHH		34.6224719451
360PhosphorylationSNAGLAVSLQLLHGD
CCHHHHHHHHHHHCC		12.5624719451
375PhosphorylationIEQIRREYSSVFSHG
HHHHHHHHHHHHHCC		12.39-
415UbiquitinationIERGEFEKGGKSVAR
EECCCEECCCEECCC		77.5832142685
506PhosphorylationEKKLFGFSFVPLMQE
CCCCCCEEEEECCCC		26.22-
563PhosphorylationNNQAMKATKESFCIT
CHHHHHHHHHHHHHH		29.8130576142
570PhosphorylationTKESFCITSFLCSTK
HHHHHHHHHHHHCCE		18.01-
571PhosphorylationKESFCITSFLCSTKL
HHHHHHHHHHHCCEE		9.0530576142
575PhosphorylationCITSFLCSTKLTQNG
HHHHHHHCCEECCCC		30.62-
576PhosphorylationITSFLCSTKLTQNGD
HHHHHHCCEECCCCC		29.1330576142
596UbiquitinationKWRTHPDKITGCLSK
HHHCCHHHHCHHHHH		46.7729967540
675PhosphorylationHFAGALAYRDLIKVL
HHHHHHHHHHHHHHH		12.90-
685PhosphorylationLIKVLKWYVDRITEA
HHHHHHHHHHHHCHH		7.2928509920
753PhosphorylationLSQESKGSGALSQSQ
HCCCCCCCCCCCHHH		25.3220071362
759PhosphorylationGSGALSQSQAVFLSS
CCCCCCHHHHHHHHC		19.4120071362
815PhosphorylationKLQCIGKTVESQLYT
HHHHCCCCHHHHHCC		25.0530619164
818PhosphorylationCIGKTVESQLYTNPD
HCCCCHHHHHCCCCC		22.5830619164
821PhosphorylationKTVESQLYTNPDSRY
CCHHHHHCCCCCCCE		9.2425884760
822PhosphorylationTVESQLYTNPDSRYI
CHHHHHCCCCCCCEE		49.2030619164
826PhosphorylationQLYTNPDSRYILLPV
HHCCCCCCCEEEHHH		28.3930619164
889PhosphorylationLLDILLRTILEITSR
HHHHHHHHHHHHHCC		29.86-
894PhosphorylationLRTILEITSRPQPSS
HHHHHHHHCCCCCCC		14.8728555341
931PhosphorylationRQMTDRHYQQLLDSF
HHHCHHHHHHHHHHC		9.9929438985
1109UbiquitinationNFKQVEAKLIDKLDS
CCHHHHHHHHHHHHH		32.2529967540
1113UbiquitinationVEAKLIDKLDSLMSE
HHHHHHHHHHHHHHC		47.3929967540
1137UbiquitinationLFNSILLKKIERETW
HHHHHHHHHHHHHHH		48.5421890473
1137 (in isoform 1)Ubiquitination-48.5421890473
1147UbiquitinationERETWRESGVSLIAT
HHHHHHHHCCHHHHH		35.6030230243
1165PhosphorylationLMERLLDYRDCMKMG
HHHHHCCHHHHHHHC		14.3418083107
1168UbiquitinationRLLDYRDCMKMGEVD
HHCCHHHHHHHCCCC		1.7721890473
1242PhosphorylationRPLREFLTYPMQTEW
CCHHHHHCCCCCCHH		30.7928450419
1243PhosphorylationPLREFLTYPMQTEWQ
CHHHHHCCCCCCHHH		10.0028450419
1247PhosphorylationFLTYPMQTEWQRKEH
HHCCCCCCHHHHCCC		32.7028450419
1283PhosphorylationCRKIAEQYESYYDYR
HHHHHHHHHHHCCCC		9.8024043423
1285PhosphorylationKIAEQYESYYDYRNL
HHHHHHHHHCCCCCH		24.8624043423
1286PhosphorylationIAEQYESYYDYRNLS
HHHHHHHHCCCCCHH		6.6024043423
1287PhosphorylationAEQYESYYDYRNLSK
HHHHHHHCCCCCHHH		18.7724043423
1289PhosphorylationQYESYYDYRNLSKMR
HHHHHCCCCCHHHHH		5.8124043423
1301PhosphorylationKMRMMEASLYDKIMD
HHHHHHHHHHHHHHH		17.73-
1485PhosphorylationNKNQQLKTLISQCQT
CHHHHHHHHHHHHHH		37.6119053533
1574UbiquitinationQDMRPLHKKLVDQFF
CCCHHHHHHHHHHHH		56.3332015554
1583UbiquitinationLVDQFFVMKSSLGIQ
HHHHHHHHHHCCCHH		2.7032015554
1599PhosphorylationFSACMQASPVHFPNG
HHHHHHCCCCCCCCC		15.5722617229
1607PhosphorylationPVHFPNGSPRVCRNS
CCCCCCCCCCCCCCC		19.0426055452
1614PhosphorylationSPRVCRNSAPASVSP
CCCCCCCCCCCCCCC		19.1021712546
1618PhosphorylationCRNSAPASVSPDGTR
CCCCCCCCCCCCCCE		23.2825159151
1620PhosphorylationNSAPASVSPDGTRVI
CCCCCCCCCCCCEEE		18.1229255136
1624PhosphorylationASVSPDGTRVIPRRS
CCCCCCCCEEECCCC		29.1929255136
1631PhosphorylationTRVIPRRSPLSYPAV
CEEECCCCCCCCCCC		31.3225159151
1634PhosphorylationIPRRSPLSYPAVNRY
ECCCCCCCCCCCCCC		32.2426657352
1635PhosphorylationPRRSPLSYPAVNRYS
CCCCCCCCCCCCCCC		11.6823403867
1640PhosphorylationLSYPAVNRYSSSSLS
CCCCCCCCCCCCCHH		26.5532142685
1641PhosphorylationSYPAVNRYSSSSLSS
CCCCCCCCCCCCHHH		14.0124275569
1643PhosphorylationPAVNRYSSSSLSSQA
CCCCCCCCCCHHHHC		18.2724275569
1700PhosphorylationAPSSARASPLLSDKH
CCCCCCCCCCCCCCC		15.5529255136
1704PhosphorylationARASPLLSDKHKHSR
CCCCCCCCCCCCCCC		52.9023403867
1710PhosphorylationLSDKHKHSRENSCLS
CCCCCCCCCCCCCCC		46.2028152594
1714PhosphorylationHKHSRENSCLSPRER
CCCCCCCCCCCCCCC		16.2229255136
1717PhosphorylationSRENSCLSPRERPCS
CCCCCCCCCCCCCCC		26.6629255136
1724PhosphorylationSPRERPCSAIYPTPV
CCCCCCCCCCCCCCC		22.0023403867
1726PhosphorylationRERPCSAIYPTPVEP
CCCCCCCCCCCCCCH		2.1333259812
1727PhosphorylationERPCSAIYPTPVEPS
CCCCCCCCCCCCCHH		10.7723403867
1729PhosphorylationPCSAIYPTPVEPSQR
CCCCCCCCCCCHHHH		24.0123403867
1734PhosphorylationYPTPVEPSQRMLFNH
CCCCCCHHHHHHHCC		19.5325072903
1750PhosphorylationGDGALPRSDPNLSAP
CCCCCCCCCCCCCCC		56.3221815630
1755PhosphorylationPRSDPNLSAPEKAVN
CCCCCCCCCCCCCCC		48.7123403867
1764PhosphorylationPEKAVNPTPSSWSLD
CCCCCCCCCCCCCCC		30.5130266825
1766PhosphorylationKAVNPTPSSWSLDSG
CCCCCCCCCCCCCCC		47.0930266825
1767PhosphorylationAVNPTPSSWSLDSGK
CCCCCCCCCCCCCCC		23.1430266825
1769PhosphorylationNPTPSSWSLDSGKEA
CCCCCCCCCCCCCCC		25.0130266825
1772PhosphorylationPSSWSLDSGKEAKNM
CCCCCCCCCCCCCCC		57.9930266825
1787PhosphorylationSDSGKLISPPVPPRP
CCCCCCCCCCCCCCC		33.3223403867
1795PhosphorylationPPVPPRPTQTASPAR
CCCCCCCCCCCCCCC		39.5723403867
1797O-linked_GlycosylationVPPRPTQTASPARHT
CCCCCCCCCCCCCCC		31.4228657654
1797PhosphorylationVPPRPTQTASPARHT
CCCCCCCCCCCCCCC		31.4223403867
1799PhosphorylationPRPTQTASPARHTTS
CCCCCCCCCCCCCCC		23.6023403867
1804PhosphorylationTASPARHTTSVSPSP
CCCCCCCCCCCCCCC		18.4029255136
1805PhosphorylationASPARHTTSVSPSPA
CCCCCCCCCCCCCCC		22.4729255136
1806PhosphorylationSPARHTTSVSPSPAG
CCCCCCCCCCCCCCC		23.0429255136
1808PhosphorylationARHTTSVSPSPAGRS
CCCCCCCCCCCCCCC		21.3029255136
1810PhosphorylationHTTSVSPSPAGRSPL
CCCCCCCCCCCCCCC		21.6329255136
1815PhosphorylationSPSPAGRSPLKGSVQ
CCCCCCCCCCCCCCC		33.4025159151
1827PhosphorylationSVQSFTPSPVEYHSP
CCCCCCCCCCEECCC		38.2221552520
1831PhosphorylationFTPSPVEYHSPGLIS
CCCCCCEECCCCCCC		14.0825884760
1833PhosphorylationPSPVEYHSPGLISNS
CCCCEECCCCCCCCC		21.5528387310
1844PhosphorylationISNSPVLSGSYSSGI
CCCCCCCCCCCCCCC		26.4028857561
1846PhosphorylationNSPVLSGSYSSGISS
CCCCCCCCCCCCCCC		20.6128857561
1847PhosphorylationSPVLSGSYSSGISSL
CCCCCCCCCCCCCCC		15.4728857561
1886PhosphorylationPVPVPVPSYGGEEPV
CCCCCCCCCCCCCCC		36.3227251275
1897PhosphorylationEEPVRKESKTPPPYS
CCCCCCCCCCCCCCC		44.8823898821
1899PhosphorylationPVRKESKTPPPYSVY
CCCCCCCCCCCCCCC		50.7528355574
1903PhosphorylationESKTPPPYSVYERTL
CCCCCCCCCCCCCCC		19.2828796482
1904PhosphorylationSKTPPPYSVYERTLR
CCCCCCCCCCCCCCC		24.8128796482
1906PhosphorylationTPPPYSVYERTLRRP
CCCCCCCCCCCCCCC		8.1828796482
1921O-linked_GlycosylationVPLPHSLSIPVTSEP
CCCCCCCCCCCCCCC		28.0628657654
1921PhosphorylationVPLPHSLSIPVTSEP
CCCCCCCCCCCCCCC		28.0628348404
1950PhosphorylationLENGARRTDPGPRPR
HHCCCCCCCCCCCCC		40.7828555341
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 DOCK4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DOCK4_HUMAN !!
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 DOCK4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HNRPL_HUMANHNRNPLphysical
17353931
GRB2_HUMANGRB2physical
21988832
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DOCK4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1614; SER-1618 ANDSER-1620, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1614; SER-1618 ANDSER-1620, AND MASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1831, AND MASSSPECTROMETRY.

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