ELMO1_HUMAN - dbPTM
ELMO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELMO1_HUMAN
UniProt AC Q92556
Protein Name Engulfment and cell motility protein 1
Gene Name ELMO1
Organism Homo sapiens (Human).
Sequence Length 727
Subcellular Localization Cytoplasm. Cell membrane. Translocation to plasma membrane seems to be mediated by DOCK1 and CRK.
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 MPPPADIVKVAIEWPGAYPKLMEIDQKKPLSAIIKEVCDGWSLANHEYFALQHADSSNFYITEKNRNEIKNGTILRLTTSPAQNAQQLHERIQSSSMDAKLEALKDLASLSRDVTFAQEFINLDGISLLTQMVESGTERYQKLQKIMKPCFGDMLSFTLTAFVELMDHGIVSWDTFSVAFIKKIASFVNKSAIDISILQRSLAILESMVLNSHDLYQKVAQEITIGQLIPHLQGSDQEIQTYTIAVINALFLKAPDERRQEMANILAQKQLRSIILTHVIRAQRAINNEMAHQLYVLQVLTFNLLEDRMMTKMDPQDQAQRDIIFELRRIAFDAESEPNNSSGSMEKRKSMYTRDYKKLGFINHVNPAMDFTQTPPGMLALDNMLYFAKHHQDAYIRIVLENSSREDKHECPFGRSSIELTKMLCEILKVGELPSETCNDFHPMFFTHDRSFEEFFCICIQLLNKTWKEMRATSEDFNKVMQVVKEQVMRALTTKPSSLDQFKSKLQNLSYTEILKIRQSERMNQEDFQSRPILELKEKIQPEILELIKQQRLNRLVEGTCFRKLNARRRQDKFWYCRLSPNHKVLHYGDLEESPQGEVPHDSLQDKLPVADIKAVVTGKDCPHMKEKGALKQNKEVLELAFSILYDSNCQLNFIAPDKHEYCIWTDGLNALLGKDMMSDLTRNDLDTLLSMEIKLRLLDLENIQIPDAPPPIPKEPSNYDFVYDCN
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
9UbiquitinationPPPADIVKVAIEWPG
CCCHHHEEEEEECCC		26.70-
18PhosphorylationAIEWPGAYPKLMEID
EEECCCCCCCHHHHC		13.5529978859
20UbiquitinationEWPGAYPKLMEIDQK
ECCCCCCCHHHHCCC		48.03-
31PhosphorylationIDQKKPLSAIIKEVC
HCCCCCHHHHHHHHH		26.4230576142
36 (in isoform 2)Ubiquitination-37.6621906983
48PhosphorylationWSLANHEYFALQHAD
CCHHCCCEEEEECCC		6.13-
70UbiquitinationEKNRNEIKNGTILRL
ECCCCCCCCCCEEEE		43.05-
78PhosphorylationNGTILRLTTSPAQNA
CCCEEEEECCHHHHH		20.8527690223
79PhosphorylationGTILRLTTSPAQNAQ
CCEEEEECCHHHHHH		36.9927690223
80PhosphorylationTILRLTTSPAQNAQQ
CEEEEECCHHHHHHH		17.0127690223
95PhosphorylationLHERIQSSSMDAKLE
HHHHHHHCCHHHHHH		17.2022210691
100AcetylationQSSSMDAKLEALKDL
HHCCHHHHHHHHHHH		42.4719608861
100UbiquitinationQSSSMDAKLEALKDL
HHCCHHHHHHHHHHH		42.4719608861
105AcetylationDAKLEALKDLASLSR
HHHHHHHHHHHHHCC		58.7119608861
105 (in isoform 1)Ubiquitination-58.7121890473
105UbiquitinationDAKLEALKDLASLSR
HHHHHHHHHHHHHCC		58.7121890473
109PhosphorylationEALKDLASLSRDVTF
HHHHHHHHHCCCCHH		33.8927174698
111PhosphorylationLKDLASLSRDVTFAQ
HHHHHHHCCCCHHHH		24.7627174698
140PhosphorylationVESGTERYQKLQKIM
HHHCHHHHHHHHHHH		12.08-
191PhosphorylationIASFVNKSAIDISIL
HHHHCCHHHHHHHHH		25.8323403867
196PhosphorylationNKSAIDISILQRSLA
CHHHHHHHHHHHHHH		17.31-
216PhosphorylationVLNSHDLYQKVAQEI
HCCCHHHHHHHHHHC		16.6122817900
218UbiquitinationNSHDLYQKVAQEITI
CCHHHHHHHHHHCCH		26.44-
269UbiquitinationMANILAQKQLRSIIL
HHHHHHHHHHHHHHH		45.77-
312UbiquitinationLEDRMMTKMDPQDQA
HHHHHHHCCCHHHHH		24.33-
328MethylationRDIIFELRRIAFDAE
HHHHHHHHHHHHCCC		22.29-
336PhosphorylationRIAFDAESEPNNSSG
HHHHCCCCCCCCCCC		61.1423403867
341PhosphorylationAESEPNNSSGSMEKR
CCCCCCCCCCCCHHH		42.5923401153
342PhosphorylationESEPNNSSGSMEKRK
CCCCCCCCCCCHHHH		36.6923401153
344PhosphorylationEPNNSSGSMEKRKSM
CCCCCCCCCHHHHHH		26.2223401153
347UbiquitinationNSSGSMEKRKSMYTR
CCCCCCHHHHHHHHC		57.39-
350PhosphorylationGSMEKRKSMYTRDYK
CCCHHHHHHHHCCHH		22.5130631047
352PhosphorylationMEKRKSMYTRDYKKL
CHHHHHHHHCCHHHH		13.00-
356PhosphorylationKSMYTRDYKKLGFIN
HHHHHCCHHHHCCCC		13.51-
395PhosphorylationAKHHQDAYIRIVLEN
HHHCCCCEEEEEEEC		10.0622817900
408UbiquitinationENSSREDKHECPFGR
ECCCCCCCCCCCCCH		36.23-
408AcetylationENSSREDKHECPFGR
ECCCCCCCCCCCCCH		36.2325825284
416PhosphorylationHECPFGRSSIELTKM
CCCCCCHHHHHHHHH		35.7322964224
417PhosphorylationECPFGRSSIELTKML
CCCCCHHHHHHHHHH		20.7922964224
422AcetylationRSSIELTKMLCEILK
HHHHHHHHHHHHHHH		42.36156515
422UbiquitinationRSSIELTKMLCEILK
HHHHHHHHHHHHHHH		42.36-
466PhosphorylationCIQLLNKTWKEMRAT
HHHHHHHHHHHHHHC		40.47-
468UbiquitinationQLLNKTWKEMRATSE
HHHHHHHHHHHHCHH		47.03-
473PhosphorylationTWKEMRATSEDFNKV
HHHHHHHCHHHHHHH		23.45-
485UbiquitinationNKVMQVVKEQVMRAL
HHHHHHHHHHHHHHH		43.50-
485AcetylationNKVMQVVKEQVMRAL
HHHHHHHHHHHHHHH		43.5012435505
503UbiquitinationPSSLDQFKSKLQNLS
CCHHHHHHHHHHCCC		40.84-
503AcetylationPSSLDQFKSKLQNLS
CCHHHHHHHHHHCCC		40.8425953088
505UbiquitinationSLDQFKSKLQNLSYT
HHHHHHHHHHCCCHH		55.47-
505AcetylationSLDQFKSKLQNLSYT
HHHHHHHHHHCCCHH		55.4725953088
510PhosphorylationKSKLQNLSYTEILKI
HHHHHCCCHHHHHHH		37.2426670566
511PhosphorylationSKLQNLSYTEILKIR
HHHHCCCHHHHHHHH		16.1426670566
512PhosphorylationKLQNLSYTEILKIRQ
HHHCCCHHHHHHHHH		17.1126670566
516UbiquitinationLSYTEILKIRQSERM
CCHHHHHHHHHHHHC		41.3121906983
516 (in isoform 1)Ubiquitination-41.3121890473
537UbiquitinationSRPILELKEKIQPEI
CCCHHHHHHHHCHHH		47.81-
539UbiquitinationPILELKEKIQPEILE
CHHHHHHHHCHHHHH		45.08-
539AcetylationPILELKEKIQPEILE
CHHHHHHHHCHHHHH		45.0825953088
549UbiquitinationPEILELIKQQRLNRL
HHHHHHHHHHHHHHH		53.67-
573AcetylationNARRRQDKFWYCRLS
CCCHHCCCCEEEEEC		29.4726822725
576PhosphorylationRRQDKFWYCRLSPNH
HHCCCCEEEEECCCC		3.19-
580PhosphorylationKFWYCRLSPNHKVLH
CCEEEEECCCCCEEE		12.3327067055
584UbiquitinationCRLSPNHKVLHYGDL
EEECCCCCEEECCCC		53.80-
588PhosphorylationPNHKVLHYGDLEESP
CCCCEEECCCCCCCC		14.2630576142
594PhosphorylationHYGDLEESPQGEVPH
ECCCCCCCCCCCCCC		17.1028122231
607UbiquitinationPHDSLQDKLPVADIK
CCCCHHCCCCHHHEE		41.55-
620UbiquitinationIKAVVTGKDCPHMKE
EEEEEECCCCHHHHH		46.95-
635AcetylationKGALKQNKEVLELAF
CCCHHHCHHHHHHHH		46.867680173
692SulfoxidationDLDTLLSMEIKLRLL
CHHHHHHHHHHHHHH		6.6021406390
695UbiquitinationTLLSMEIKLRLLDLE
HHHHHHHHHHHHCCC		17.78-
718PhosphorylationPPIPKEPSNYDFVYD
CCCCCCCCCCCCCEE		49.4628796482
720PhosphorylationIPKEPSNYDFVYDCN
CCCCCCCCCCCEECC		18.3320869035
724PhosphorylationPSNYDFVYDCN----
CCCCCCCEECC----		18.1228796482
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
18YPhosphorylationKinaseHCKP08631
Uniprot
216YPhosphorylationKinaseHCKP08631
Uniprot
395YPhosphorylationKinaseHCKP08631
Uniprot
511YPhosphorylationKinaseHCKP08631
Uniprot
720YPhosphorylationKinaseHCKP08631
Uniprot
720YPhosphorylationKinaseSRCP12931
PSP
720YPhosphorylationKinaseAXLP30530
PSP
724YPhosphorylationKinaseSRCP12931
PSP
724YPhosphorylationKinaseAXLP30530
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELMO1_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 ELMO1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DOCK1_HUMANDOCK1physical
11595183
DOCK1_HUMANDOCK1physical
12134158
DOCK1_HUMANDOCK1physical
16495483
PGH2_HUMANPTGS2physical
20732417
DOCK1_HUMANDOCK1physical
20732417
TRI54_HUMANTRIM54physical
25416956
ZN398_HUMANZNF398physical
25416956
DOCK4_HUMANDOCK4physical
26186194
DOCK3_HUMANDOCK3physical
26186194
UBP4_HUMANUSP4physical
26186194
MED31_HUMANMED31physical
26186194
DOCK5_HUMANDOCK5physical
26186194
DOCK1_HUMANDOCK1physical
26186194
TTC19_HUMANTTC19physical
26186194
ELMO2_HUMANELMO2physical
26186194
ZN398_HUMANZNF398physical
26186194
CALL3_HUMANCALML3physical
26186194
RHOG_HUMANRHOGphysical
21930703
DOCK1_HUMANDOCK1physical
21930703
DOCK2_HUMANDOCK2physical
21930703
DOCK3_HUMANDOCK3physical
21930703
DOCK4_HUMANDOCK4physical
21930703
DOCK5_HUMANDOCK5physical
21930703
AGRB1_HUMANBAI1physical
21930703
AGRB3_HUMANBAI3physical
21930703
ARL4A_HUMANARL4Aphysical
21930703
CDC27_HUMANCDC27physical
26882976
DOCK1_HUMANDOCK1physical
26882976
DOCK5_HUMANDOCK5physical
28514442
DOCK4_HUMANDOCK4physical
28514442
DOCK1_HUMANDOCK1physical
28514442
DOCK3_HUMANDOCK3physical
28514442
ELMO2_HUMANELMO2physical
28514442
ZN398_HUMANZNF398physical
28514442
UBP4_HUMANUSP4physical
28514442
MED31_HUMANMED31physical
28514442
CALL3_HUMANCALML3physical
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 ELMO1_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-100 AND LYS-105, AND MASSSPECTROMETRY.
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-344, AND MASSSPECTROMETRY.
"Identification of tyrosine residues on ELMO1 that are phosphorylatedby the Src-family kinase Hck.";
Yokoyama N., deBakker C.D., Zappacosta F., Huddleston M.J.,Annan R.S., Ravichandran K.S., Miller W.T.;
Biochemistry 44:8841-8849(2005).
Cited for: INTERACTION WITH HCK, AND PHOSPHORYLATION AT TYR-18; TYR-216; TYR-395;TYR-511 AND TYR-720.

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