DOCK5_HUMAN - dbPTM
DOCK5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DOCK5_HUMAN
UniProt AC Q9H7D0
Protein Name Dedicator of cytokinesis protein 5
Gene Name DOCK5
Organism Homo sapiens (Human).
Sequence Length 1870
Subcellular Localization Cytoplasm . Cell membrane . Associated with the edge of the plasma membrane in Caco-2 intestinal epithelial cells spreading on type IV collagen.
Protein Description Guanine nucleotide exchange factor (GEF) for Rho and Rac. GEF proteins activate small GTPases by exchanging bound GDP for free GTP (By similarity). Along with DOCK1, mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on type IV collagen. [PubMed: 19004829]
Protein Sequence MARWIPTKRQKYGVAIYNYNASQDVELSLQIGDTVHILEMYEGWYRGYTLQNKSKKGIFPETYIHLKEATVEDLGQHETVIPGELPLVQELTSTLREWAVIWRKLYVNNKLTLFRQLQQMTYSLIEWRSQILSGTLPKDELAELKKKVTAKIDHGNRMLGLDLVVRDDNGNILDPDETSTIALFKAHEVASKRIEEKIQEEKSILQNLDLRGQSIFSTIHTYGLYVNFKNFVCNIGEDAELFMALYDPDQSTFISENYLIRWGSNGMPKEIEKLNNLQAVFTDLSSMDLIRPRVSLVCQIVRVGHMELKEGKKHTCGLRRPFGVAVMDITDIIHGKVDDEEKQHFIPFQQIAMETYIRQRQLIMSPLITSHVIGENEPLTSVLNKVIAAKEVNHKGQGLWVSLKLLPGDLTQVQKNFSHLVDRSTAIARKMGFPEIILPGDVRNDIYVTLIHGEFDKGKKKTPKNVEVTMSVHDEEGKLLEKAIHPGAGYEGISEYKSVVYYQVKQPCWYETVKVSIAIEEVTRCHIRFTFRHRSSQETRDKSERAFGVAFVKLMNPDGTTLQDGRHDLVVYKGDNKKMEDAKFYLTLPGTKMEMEEKELQASKNLVTFTPSKDSTKDSFQIATLICSTKLTQNVDLLGLLNWRSNSQNIKHNLKKLMEVDGGEIVKFLQDTLDALFNIMMEMSDSETYDFLVFDALVFIISLIGDIKFQHFNPVLETYIYKHFSATLAYVKLSKVLNFYVANADDSSKTELLFAALKALKYLFRFIIQSRVLYLRFYGQSKDGDEFNNSIRQLFLAFNMLMDRPLEEAVKIKGAALKYLPSIINDVKLVFDPVELSVLFCKFIQSIPDNQLVRQKLNCMTKIVESTLFRQSECREVLLPLLTDQLSGQLDDNSNKPDHEASSQLLSNILEVLDRKDVGATAVHIQLIMERLLRRINRTVIGMNRQSPHIGSFVACMIALLQQMDDSHYSHYISTFKTRQDIIDFLMETFIMFKDLIGKNVYAKDWMVMNMTQNRVFLRAINQFAEVLTRFFMDQASFELQLWNNYFHLAVAFLTHESLQLETFSQAKRNKIVKKYGDMRKEIGFRIRDMWYNLGPHKIKFIPSMVGPILEVTLTPEVELRKATIPIFFDMMQCEFNFSGNGNFHMFENELITKLDQEVEGGRGDEQYKVLLEKLLLEHCRKHKYLSSSGEVFALLVSSLLENLLDYRTIIMQDESKENRMSCTVNVLNFYKEKKREDIYIRYLYKLRDLHRDCENYTEAAYTLLLHAELLQWSDKPCVPHLLQKDSYYVYTQQELKEKLYQEIISYFDKGKMWEKAIKLSKELAETYESKVFDYEGLGNLLKKRASFYENIIKAMRPQPEYFAVGYYGQGFPSFLRNKIFIYRGKEYERREDFSLRLLTQFPNAEKMTSTTPPGEDIKSSPKQYMQCFTVKPVMSLPPSYKDKPVPEQILNYYRANEVQQFRYSRPFRKGEKDPDNEFATMWIERTTYTTAYTFPGILKWFEVKQISTEEISPLENAIETMELTNERISNCVQQHAWDRSLSVHPLSMLLSGIVDPAVMGGFSNYEKAFFTEKYLQEHPEDQEKVELLKRLIALQMPLLTEGIRIHGEKLTEQLKPLHERLSSCFRELKEKVEKHYGVITLPPNLTERKQSRTGSIVLPYIMSSTLRRLSITSVTSSVVSTSSNSSDNAPSRPGSDGSILEPLLERRASSGARVEDLSLREENSENRISKFKRKDWSLSKSQVIAEKAPEPDLMSPTRKAQRPKSLQLMDNRLSPFHGSSPPQSTPLSPPPLTPKATRTLSSPSLQTDGIAATPVPPPPPPKSKPYEGSQRNSTELAPPLPVRREAKAPPPPPPKARKSGIPTSEPGSQ
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
53UbiquitinationRGYTLQNKSKKGIFP
HCCCCCCCCCCCCCC
51.17-
56MalonylationTLQNKSKKGIFPETY
CCCCCCCCCCCCHHE
65.4126320211
63PhosphorylationKGIFPETYIHLKEAT
CCCCCHHEEEEEEEE
5.6727642862
106PhosphorylationAVIWRKLYVNNKLTL
HHHHHHHHHCCHHHH
12.27-
121PhosphorylationFRQLQQMTYSLIEWR
HHHHHHHHHHHHHHH
12.9620068231
122PhosphorylationRQLQQMTYSLIEWRS
HHHHHHHHHHHHHHH
8.9920068231
123PhosphorylationQLQQMTYSLIEWRSQ
HHHHHHHHHHHHHHH
17.4428464451
129PhosphorylationYSLIEWRSQILSGTL
HHHHHHHHHHHHCCC
23.7328464451
133PhosphorylationEWRSQILSGTLPKDE
HHHHHHHHCCCCHHH
31.2120068231
135PhosphorylationRSQILSGTLPKDELA
HHHHHHCCCCHHHHH
36.1920068231
145UbiquitinationKDELAELKKKVTAKI
HHHHHHHHHHHEEEE
41.89-
151UbiquitinationLKKKVTAKIDHGNRM
HHHHHEEEECCCCCE
39.02-
185UbiquitinationTSTIALFKAHEVASK
CHHHHHHHHHHHHHH
50.08-
202UbiquitinationEEKIQEEKSILQNLD
HHHHHHHHHHHHCCC
41.88-
342UbiquitinationGKVDDEEKQHFIPFQ
CCCCHHHHHHCCCHH
47.20-
365PhosphorylationRQRQLIMSPLITSHV
HHHHHHCCHHHHHHC
15.0121712546
369PhosphorylationLIMSPLITSHVIGEN
HHCCHHHHHHCCCCC
22.0628450419
370PhosphorylationIMSPLITSHVIGENE
HCCHHHHHHCCCCCC
14.5728450419
390UbiquitinationLNKVIAAKEVNHKGQ
HHHHHHHHHCCCCCC
53.85-
395UbiquitinationAAKEVNHKGQGLWVS
HHHHCCCCCCCEEEE
47.96-
415UbiquitinationGDLTQVQKNFSHLVD
CCHHHHHHHHHHHHC
62.19-
418PhosphorylationTQVQKNFSHLVDRST
HHHHHHHHHHHCHHH
25.8828270605
482UbiquitinationEEGKLLEKAIHPGAG
CCCCCHHHHCCCCCC
53.24-
497AcetylationYEGISEYKSVVYYQV
CCCHHHCCEEEEEEE
32.4926051181
573UbiquitinationRHDLVVYKGDNKKME
CCEEEEEECCCCCEE
48.45-
604UbiquitinationEKELQASKNLVTFTP
HHHHHHCCCEEEECC
58.26-
608PhosphorylationQASKNLVTFTPSKDS
HHCCCEEEECCCCCC
25.5929396449
610PhosphorylationSKNLVTFTPSKDSTK
CCCEEEECCCCCCCC
19.7925159151
612PhosphorylationNLVTFTPSKDSTKDS
CEEEECCCCCCCCCH
46.1429396449
615PhosphorylationTFTPSKDSTKDSFQI
EECCCCCCCCCHHHH
40.8823186163
616PhosphorylationFTPSKDSTKDSFQIA
ECCCCCCCCCHHHHH
49.3423186163
619PhosphorylationSKDSTKDSFQIATLI
CCCCCCCHHHHHHHH
22.17-
624PhosphorylationKDSFQIATLICSTKL
CCHHHHHHHHHCCCC
20.48-
645PhosphorylationLGLLNWRSNSQNIKH
HHHHCCCCCCHHHHH
32.2327174698
647PhosphorylationLLNWRSNSQNIKHNL
HHCCCCCCHHHHHHH
26.3327174698
651UbiquitinationRSNSQNIKHNLKKLM
CCCCHHHHHHHHHHH
33.71-
818AcetylationKIKGAALKYLPSIIN
HHCHHHHHHHHHHHC
39.7619608861
818UbiquitinationKIKGAALKYLPSIIN
HHCHHHHHHHHHHHC
39.7619608861
819PhosphorylationIKGAALKYLPSIIND
HCHHHHHHHHHHHCC
25.3724114839
822PhosphorylationAALKYLPSIINDVKL
HHHHHHHHHHCCEEE
33.2424114839
856UbiquitinationDNQLVRQKLNCMTKI
CHHHHHHHHHHHHHH
30.97-
999UbiquitinationMFKDLIGKNVYAKDW
HHHHHCCCCCCCCCC
35.92-
1019DimethylationTQNRVFLRAINQFAE
CCCHHHHHHHHHHHH
23.20-
1124PhosphorylationEVELRKATIPIFFDM
CHHHHHCCCCEEEEE
30.2624043423
1139PhosphorylationMQCEFNFSGNGNFHM
ECCEEECCCCCCEEE
32.2424043423
1153PhosphorylationMFENELITKLDQEVE
EEECEEHHHHHHHHC
37.8724043423
1169UbiquitinationGRGDEQYKVLLEKLL
CCCHHHHHHHHHHHH
26.54-
1198PhosphorylationEVFALLVSSLLENLL
HHHHHHHHHHHHHHC
18.42-
1222PhosphorylationESKENRMSCTVNVLN
CCHHHHHCCEEEHHH
11.9122496350
1224PhosphorylationKENRMSCTVNVLNFY
HHHHHCCEEEHHHHH
14.07-
1246UbiquitinationIYIRYLYKLRDLHRD
HHHHHHHHHHHHHHC
34.16-
1287PhosphorylationPHLLQKDSYYVYTQQ
HHHHCCCCEEEEEHH
25.9621945579
1288PhosphorylationHLLQKDSYYVYTQQE
HHHCCCCEEEEEHHH
13.6921945579
1289PhosphorylationLLQKDSYYVYTQQEL
HHCCCCEEEEEHHHH
7.3121945579
1291PhosphorylationQKDSYYVYTQQELKE
CCCCEEEEEHHHHHH
5.2321945579
1292PhosphorylationKDSYYVYTQQELKEK
CCCEEEEEHHHHHHH
17.4621945579
1316UbiquitinationDKGKMWEKAIKLSKE
HHCHHHHHHHHHHHH
39.64-
1322UbiquitinationEKAIKLSKELAETYE
HHHHHHHHHHHHHHH
68.15-
1331UbiquitinationLAETYESKVFDYEGL
HHHHHHHHCCCHHCH
34.67-
1343UbiquitinationEGLGNLLKKRASFYE
HCHHHHHHHHHHHHH
43.30-
1347PhosphorylationNLLKKRASFYENIIK
HHHHHHHHHHHHHHH
32.1825159151
1349PhosphorylationLKKRASFYENIIKAM
HHHHHHHHHHHHHHH
12.9328152594
1395PhosphorylationYERREDFSLRLLTQF
CCCCCCCCHHHHHCC
25.54-
1407UbiquitinationTQFPNAEKMTSTTPP
HCCCCHHHCCCCCCC
45.10-
1409PhosphorylationFPNAEKMTSTTPPGE
CCCHHHCCCCCCCCC
33.7127732954
1410PhosphorylationPNAEKMTSTTPPGED
CCHHHCCCCCCCCCC
27.1327732954
1411PhosphorylationNAEKMTSTTPPGEDI
CHHHCCCCCCCCCCC
33.8727732954
1412PhosphorylationAEKMTSTTPPGEDIK
HHHCCCCCCCCCCCC
27.5321815630
1444UbiquitinationLPPSYKDKPVPEQIL
CCCCCCCCCCCHHHH
43.70-
1453PhosphorylationVPEQILNYYRANEVQ
CCHHHHHHHHHCCCH
7.2928634298
1454PhosphorylationPEQILNYYRANEVQQ
CHHHHHHHHHCCCHH
11.3728634298
1574UbiquitinationEKAFFTEKYLQEHPE
HHHHHHHHHHHHCCC
48.48-
1585UbiquitinationEHPEDQEKVELLKRL
HCCCHHHHHHHHHHH
35.06-
1601PhosphorylationALQMPLLTEGIRIHG
HHHCHHHCCCCCCCH
39.59-
1616UbiquitinationEKLTEQLKPLHERLS
HHHHHHHHHHHHHHH
45.27-
1637PhosphorylationKEKVEKHYGVITLPP
HHHHHHHCEEEECCC
24.9324719451
1641PhosphorylationEKHYGVITLPPNLTE
HHHCEEEECCCCCCC
30.7024719451
1652PhosphorylationNLTERKQSRTGSIVL
CCCCCCCCCCCCCHH
34.5429978859
1654PhosphorylationTERKQSRTGSIVLPY
CCCCCCCCCCCHHHH
40.2921945579
1656PhosphorylationRKQSRTGSIVLPYIM
CCCCCCCCCHHHHHH
14.6521945579
1661PhosphorylationTGSIVLPYIMSSTLR
CCCCHHHHHHHHHHH
12.7021945579
1664PhosphorylationIVLPYIMSSTLRRLS
CHHHHHHHHHHHHEE
15.6021945579
1665PhosphorylationVLPYIMSSTLRRLSI
HHHHHHHHHHHHEEC
17.6821945579
1666PhosphorylationLPYIMSSTLRRLSIT
HHHHHHHHHHHEECE
19.5821945579
1671PhosphorylationSSTLRRLSITSVTSS
HHHHHHEECEEEEEE
23.2426657352
1673PhosphorylationTLRRLSITSVTSSVV
HHHHEECEEEEEEEE
17.4825849741
1674PhosphorylationLRRLSITSVTSSVVS
HHHEECEEEEEEEEE
23.0225002506
1676PhosphorylationRLSITSVTSSVVSTS
HEECEEEEEEEEECC
18.3024247654
1677PhosphorylationLSITSVTSSVVSTSS
EECEEEEEEEEECCC
20.9827080861
1678PhosphorylationSITSVTSSVVSTSSN
ECEEEEEEEEECCCC
19.7127080861
1681PhosphorylationSVTSSVVSTSSNSSD
EEEEEEEECCCCCCC
22.0327080861
1682PhosphorylationVTSSVVSTSSNSSDN
EEEEEEECCCCCCCC
25.2727080861
1683PhosphorylationTSSVVSTSSNSSDNA
EEEEEECCCCCCCCC
21.7327080861
1684PhosphorylationSSVVSTSSNSSDNAP
EEEEECCCCCCCCCC
40.6027080861
1686PhosphorylationVVSTSSNSSDNAPSR
EEECCCCCCCCCCCC
40.8027080861
1687PhosphorylationVSTSSNSSDNAPSRP
EECCCCCCCCCCCCC
38.8525002506
1692PhosphorylationNSSDNAPSRPGSDGS
CCCCCCCCCCCCCCC
49.0127080861
1696PhosphorylationNAPSRPGSDGSILEP
CCCCCCCCCCCCHHH
41.2927080861
1699PhosphorylationSRPGSDGSILEPLLE
CCCCCCCCCHHHHHH
29.0527080861
1710PhosphorylationPLLERRASSGARVED
HHHHHHHHCCCCHHH
27.7426329039
1711PhosphorylationLLERRASSGARVEDL
HHHHHHHCCCCHHHC
35.1726329039
1719PhosphorylationGARVEDLSLREENSE
CCCHHHCCCCCCCCC
37.3921815630
1725PhosphorylationLSLREENSENRISKF
CCCCCCCCCCCHHHC
39.2621712546
1738PhosphorylationKFKRKDWSLSKSQVI
HCHHCCCCCCHHHHH
32.6623403867
1740PhosphorylationKRKDWSLSKSQVIAE
HHCCCCCCHHHHHHH
25.4223403867
1741UbiquitinationRKDWSLSKSQVIAEK
HCCCCCCHHHHHHHH
50.64-
1742PhosphorylationKDWSLSKSQVIAEKA
CCCCCCHHHHHHHHC
26.7223927012
1755SulfoxidationKAPEPDLMSPTRKAQ
HCCCCCCCCCCCCCC
6.1730846556
1756PhosphorylationAPEPDLMSPTRKAQR
CCCCCCCCCCCCCCC
30.3423401153
1758PhosphorylationEPDLMSPTRKAQRPK
CCCCCCCCCCCCCCC
37.1829255136
1766PhosphorylationRKAQRPKSLQLMDNR
CCCCCCCCCCCCCCC
24.8329255136
1775PhosphorylationQLMDNRLSPFHGSSP
CCCCCCCCCCCCCCC
23.4523927012
1780PhosphorylationRLSPFHGSSPPQSTP
CCCCCCCCCCCCCCC
30.9723927012
1781PhosphorylationLSPFHGSSPPQSTPL
CCCCCCCCCCCCCCC
45.2323927012
1785PhosphorylationHGSSPPQSTPLSPPP
CCCCCCCCCCCCCCC
37.4523927012
1786PhosphorylationGSSPPQSTPLSPPPL
CCCCCCCCCCCCCCC
24.0123927012
1789PhosphorylationPPQSTPLSPPPLTPK
CCCCCCCCCCCCCCC
36.2429255136
1794PhosphorylationPLSPPPLTPKATRTL
CCCCCCCCCCCCCCC
28.6329255136
1798PhosphorylationPPLTPKATRTLSSPS
CCCCCCCCCCCCCCC
30.2529514088
1800PhosphorylationLTPKATRTLSSPSLQ
CCCCCCCCCCCCCCC
27.0030266825
1802PhosphorylationPKATRTLSSPSLQTD
CCCCCCCCCCCCCCC
39.3230266825
1803PhosphorylationKATRTLSSPSLQTDG
CCCCCCCCCCCCCCC
22.9430266825
1805PhosphorylationTRTLSSPSLQTDGIA
CCCCCCCCCCCCCCC
34.7530266825
1808PhosphorylationLSSPSLQTDGIAATP
CCCCCCCCCCCCCCC
41.3030278072
1814PhosphorylationQTDGIAATPVPPPPP
CCCCCCCCCCCCCCC
18.7925159151
1824PhosphorylationPPPPPPKSKPYEGSQ
CCCCCCCCCCCCCCC
44.6428152594
1827PhosphorylationPPPKSKPYEGSQRNS
CCCCCCCCCCCCCCC
36.3428152594
1830PhosphorylationKSKPYEGSQRNSTEL
CCCCCCCCCCCCCCC
17.6425159151
1834PhosphorylationYEGSQRNSTELAPPL
CCCCCCCCCCCCCCC
26.0029255136
1835PhosphorylationEGSQRNSTELAPPLP
CCCCCCCCCCCCCCC
38.2730266825
1860PhosphorylationPPPKARKSGIPTSEP
CCCCHHHCCCCCCCC
36.0830266825
1864PhosphorylationARKSGIPTSEPGSQ-
HHHCCCCCCCCCCC-
43.7530266825
1865O-linked_GlycosylationRKSGIPTSEPGSQ--
HHCCCCCCCCCCC--
36.1228657654
1865PhosphorylationRKSGIPTSEPGSQ--
HHCCCCCCCCCCC--
36.1230266825
1869PhosphorylationIPTSEPGSQ------
CCCCCCCCC------
43.3530266825

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 DOCK5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DOCK5_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 DOCK5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELMO2_HUMANELMO2physical
28514442
ZHX2_HUMANZHX2physical
28514442
AT1A2_HUMANATP1A2physical
28514442
TBB1_HUMANTUBB1physical
28514442
ANR54_HUMANANKRD54physical
28514442
DDX11_HUMANDDX11physical
28514442
TGON2_HUMANTGOLN2physical
28514442
AHI1_HUMANAHI1physical
28514442
MYCB2_HUMANMYCBP2physical
28514442
GPN2_HUMANGPN2physical
28514442
SPSB3_HUMANSPSB3physical
28514442
CE034_HUMANC5orf34physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
HDAC6_HUMANHDAC6physical
28514442
TBB3_HUMANTUBB3physical
28514442
MKS1_HUMANMKS1physical
28514442
MOCOS_HUMANMOCOSphysical
28514442
K0100_HUMANKIAA0100physical
28514442
WDR59_HUMANWDR59physical
28514442
DPYL4_HUMANDPYSL4physical
28514442
METH_HUMANMTRphysical
28514442
RN5A_HUMANRNASELphysical
28514442
NOL11_HUMANNOL11physical
28514442
VP13B_HUMANVPS13Bphysical
28514442
MADD_HUMANMADDphysical
28514442
PKHG4_HUMANPLEKHG4physical
28514442
TRI65_HUMANTRIM65physical
28514442
FANCJ_HUMANBRIP1physical
28514442
K0232_HUMANKIAA0232physical
28514442
TTC28_HUMANTTC28physical
28514442
UBP19_HUMANUSP19physical
28514442
BCAS3_HUMANBCAS3physical
28514442
RB3GP_HUMANRAB3GAP1physical
28514442
ATG2B_HUMANATG2Bphysical
28514442
WDR19_HUMANWDR19physical
28514442
SMG8_HUMANSMG8physical
28514442
LRCH2_HUMANLRCH2physical
28514442
PJA1_HUMANPJA1physical
28514442
STIL_HUMANSTILphysical
28514442
HSP7C_HUMANHSPA8physical
28514442
PK3CB_HUMANPIK3CBphysical
28514442
MICU1_HUMANMICU1physical
28514442
KIF1A_HUMANKIF1Aphysical
28514442
SZT2_HUMANSZT2physical
28514442
KPCD2_HUMANPRKD2physical
28514442

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 DOCK5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-818, AND MASS SPECTROMETRY.
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-1834, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1756 AND SER-1789, ANDMASS 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-1766; SER-1789;THR-1794; SER-1834 AND SER-1869, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-1756; SER-1789AND SER-1869, AND MASS SPECTROMETRY.

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