ELMO2_HUMAN - dbPTM
ELMO2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELMO2_HUMAN
UniProt AC Q96JJ3
Protein Name Engulfment and cell motility protein 2
Gene Name ELMO2
Organism Homo sapiens (Human).
Sequence Length 720
Subcellular Localization Cytoplasm . Cytoplasm, cytosol . Membrane .
Protein Description Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in association with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1..
Protein Sequence MPPPSDIVKVAIEWPGANAQLLEIDQKRPLASIIKEVCDGWSLPNPEYYTLRYADGPQLYITEQTRSDIKNGTILQLAISPSRAARQLMERTQSSNMETRLDAMKELAKLSADVTFATEFINMDGIIVLTRLVESGTKLLSHYSEMLAFTLTAFLELMDHGIVSWDMVSITFIKQIAGYVSQPMVDVSILQRSLAILESMVLNSQSLYQKIAEEITVGQLISHLQVSNQEIQTYAIALINALFLKAPEDKRQDMANAFAQKHLRSIILNHVIRGNRPIKTEMAHQLYVLQVLTFNLLEERMMTKMDPNDQAQRDIIFELRRIAFDAESDPSNAPGSGTEKRKAMYTKDYKMLGFTNHINPAMDFTQTPPGMLALDNMLYLAKVHQDTYIRIVLENSSREDKHECPFGRSAIELTKMLCEILQVGELPNEGRNDYHPMFFTHDRAFEELFGICIQLLNKTWKEMRATAEDFNKVMQVVREQITRALPSKPNSLDQFKSKLRSLSYSEILRLRQSERMSQDDFQSPPIVELREKIQPEILELIKQQRLNRLCEGSSFRKIGNRRRQERFWYCRLALNHKVLHYGDLDDNPQGEVTFESLQEKIPVADIKAIVTGKDCPHMKEKSALKQNKEVLELAFSILYDPDETLNFIAPNKYEYCIWIDGLSALLGKDMSSELTKSDLDTLLSMEMKLRLLDLENIQIPEAPPPIPKEPSSYDFVYHYG
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
17UbiquitinationVAIEWPGANAQLLEI
EEEECCCCCCHHEEH		12.2429967540
32PhosphorylationDQKRPLASIIKEVCD
HHCCCHHHHHHHHHC		32.3124719451
42PhosphorylationKEVCDGWSLPNPEYY
HHHHCCCCCCCCCCE		39.2126356563
48PhosphorylationWSLPNPEYYTLRYAD
CCCCCCCCEEEEECC		11.7421082442
49PhosphorylationSLPNPEYYTLRYADG
CCCCCCCEEEEECCC		9.5326356563
50PhosphorylationLPNPEYYTLRYADGP
CCCCCCEEEEECCCC		12.1227259358
53PhosphorylationPEYYTLRYADGPQLY
CCCEEEEECCCCEEE		16.5023898821
60PhosphorylationYADGPQLYITEQTRS
ECCCCEEEEEECCHH		10.6823898821
62PhosphorylationDGPQLYITEQTRSDI
CCCEEEEEECCHHHC		14.4223898821
65PhosphorylationQLYITEQTRSDIKNG
EEEEEECCHHHCCCC		26.3823898821
80PhosphorylationTILQLAISPSRAARQ
EEEEEEECHHHHHHH		15.9428555341
105UbiquitinationETRLDAMKELAKLSA
HHHHHHHHHHHHHCC		51.8229967540
121UbiquitinationVTFATEFINMDGIIV
CEEECCCCCCCCEEE		3.2124816145
199PhosphorylationRSLAILESMVLNSQS
HHHHHHHHHHHCCHH		15.6727690223
204PhosphorylationLESMVLNSQSLYQKI
HHHHHHCCHHHHHHH		19.5827690223
206PhosphorylationSMVLNSQSLYQKIAE
HHHHCCHHHHHHHHH		28.9427690223
208PhosphorylationVLNSQSLYQKIAEEI
HHCCHHHHHHHHHHC		17.0127690223
216UbiquitinationQKIAEEITVGQLISH
HHHHHHCCHHHHHHH		23.1224816145
218UbiquitinationIAEEITVGQLISHLQ
HHHHCCHHHHHHHCC		14.1324816145
252UbiquitinationKAPEDKRQDMANAFA
CCCHHHHHHHHHHHH		51.0421906983
252UbiquitinationKAPEDKRQDMANAFA
CCCHHHHHHHHHHHH		51.0430230243
304UbiquitinationLEERMMTKMDPNDQA
HHHHHHCCCCCCHHH		24.3324816145
313UbiquitinationDPNDQAQRDIIFELR
CCCHHHHHHHHHHHH		39.8624816145
320MethylationRDIIFELRRIAFDAE
HHHHHHHHHHHHCCC		22.29-
328PhosphorylationRIAFDAESDPSNAPG
HHHHCCCCCCCCCCC		57.4520068231
331PhosphorylationFDAESDPSNAPGSGT
HCCCCCCCCCCCCCC		51.0920068231
336PhosphorylationDPSNAPGSGTEKRKA
CCCCCCCCCCHHHHH		41.2925159151
338PhosphorylationSNAPGSGTEKRKAMY
CCCCCCCCHHHHHEE		39.7825159151
340UbiquitinationAPGSGTEKRKAMYTK
CCCCCCHHHHHEECC		60.0629967540
347UbiquitinationKRKAMYTKDYKMLGF
HHHHEECCCCHHCCC		41.39-
349UbiquitinationKAMYTKDYKMLGFTN
HHEECCCCHHCCCCC		10.3922505724
349PhosphorylationKAMYTKDYKMLGFTN
HHEECCCCHHCCCCC		10.3922817900
352 (in isoform 1)Ubiquitination-4.4521906983
359UbiquitinationLGFTNHINPAMDFTQ
CCCCCCCCCCCCCCC		15.6622505724
387PhosphorylationLAKVHQDTYIRIVLE
HHHHCCCCEEEEEEE		17.8020860994
388PhosphorylationAKVHQDTYIRIVLEN
HHHCCCCEEEEEEEC		9.1120860994
400UbiquitinationLENSSREDKHECPFG
EECCCCCCCCCCCCC		57.4029967540
401UbiquitinationENSSREDKHECPFGR
ECCCCCCCCCCCCCH		36.2324816145
401AcetylationENSSREDKHECPFGR
ECCCCCCCCCCCCCH		36.23-
408UbiquitinationKHECPFGRSAIELTK
CCCCCCCHHHHHHHH		24.2429967540
415AcetylationRSAIELTKMLCEILQ
HHHHHHHHHHHHHHH		42.36156507
444UbiquitinationMFFTHDRAFEELFGI
CCCCCHHHHHHHHHH		23.4322505724
454UbiquitinationELFGICIQLLNKTWK
HHHHHHHHHHHHHHH		35.1722505724
459PhosphorylationCIQLLNKTWKEMRAT
HHHHHHHHHHHHHHC		40.47-
461UbiquitinationQLLNKTWKEMRATAE
HHHHHHHHHHHHCHH		47.03-
487PhosphorylationQITRALPSKPNSLDQ
HHHHHCCCCCCCHHH		62.6924719451
488UbiquitinationITRALPSKPNSLDQF
HHHHCCCCCCCHHHH		46.4029967540
496UbiquitinationPNSLDQFKSKLRSLS
CCCHHHHHHHHHHCC		40.8429967540
501PhosphorylationQFKSKLRSLSYSEIL
HHHHHHHHCCHHHHH		31.9123403867
503PhosphorylationKSKLRSLSYSEILRL
HHHHHHCCHHHHHHH		28.0522115753
504PhosphorylationSKLRSLSYSEILRLR
HHHHHCCHHHHHHHH		18.6723403867
505PhosphorylationKLRSLSYSEILRLRQ
HHHHCCHHHHHHHHH		18.1323403867
512UbiquitinationSEILRLRQSERMSQD
HHHHHHHHHHHCCCC		54.9929967540
513PhosphorylationEILRLRQSERMSQDD
HHHHHHHHHHCCCCC		22.2722496350
517PhosphorylationLRQSERMSQDDFQSP
HHHHHHCCCCCCCCC		36.3622496350
519UbiquitinationQSERMSQDDFQSPPI
HHHHCCCCCCCCCCH		51.9232015554
523PhosphorylationMSQDDFQSPPIVELR
CCCCCCCCCCHHHHH		32.4121815630
525UbiquitinationQDDFQSPPIVELREK
CCCCCCCCHHHHHHH		48.8029967540
532UbiquitinationPIVELREKIQPEILE
CHHHHHHHHCHHHHH		39.9622505724
542UbiquitinationPEILELIKQQRLNRL
HHHHHHHHHHHHHHH		53.6722505724
553PhosphorylationLNRLCEGSSFRKIGN
HHHHCCCCCHHCCCC		12.1930108239
554PhosphorylationNRLCEGSSFRKIGNR
HHHCCCCCHHCCCCH		39.6730108239
577UbiquitinationCRLALNHKVLHYGDL
HHHHHCCCEEECCCC		45.47-
600UbiquitinationTFESLQEKIPVADIK
EHHHHHHHCCHHHEE		39.0729967540
607UbiquitinationKIPVADIKAIVTGKD
HCCHHHEEEHHHCCC		32.3832015554
611PhosphorylationADIKAIVTGKDCPHM
HHEEEHHHCCCCCCH		32.19-
613UbiquitinationIKAIVTGKDCPHMKE
EEEHHHCCCCCCHHH		46.9529967540
625AcetylationMKEKSALKQNKEVLE
HHHHHHHHHCHHHHH		52.0925953088
685SulfoxidationDLDTLLSMEMKLRLL
HHHHHHCHHHHHHHH		6.1830846556
687SulfoxidationDTLLSMEMKLRLLDL
HHHHCHHHHHHHHCH		3.5730846556
688UbiquitinationTLLSMEMKLRLLDLE
HHHCHHHHHHHHCHH		19.6929967540
711PhosphorylationPPIPKEPSSYDFVYH
CCCCCCCCCCCCCCC		42.4928152594
712PhosphorylationPIPKEPSSYDFVYHY
CCCCCCCCCCCCCCC		39.1628796482
713PhosphorylationIPKEPSSYDFVYHYG
CCCCCCCCCCCCCCC		20.1028796482
717PhosphorylationPSSYDFVYHYG----
CCCCCCCCCCC----		6.8519605366
719PhosphorylationSYDFVYHYG------
CCCCCCCCC------		13.5721082442
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
713YPhosphorylationKinaseAXLP30530
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELMO2_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 ELMO2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARL4A_HUMANARL4Aphysical
21930703
CDC27_HUMANCDC27physical
26882976
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 ELMO2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-48 AND TYR-717, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-48, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-48, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-48, AND MASSSPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-48, AND MASSSPECTROMETRY.

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