ELMO1_MOUSE - dbPTM
ELMO1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELMO1_MOUSE
UniProt AC Q8BPU7
Protein Name Engulfment and cell motility protein 1
Gene Name Elmo1
Organism Mus musculus (Mouse).
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 (By similarity)..
Protein Sequence MPPPSDIVKVAIEWPGAYPKLMEIDQKKPLSAIIKEVCDGWSLANHEYFALQHADSSNFYITEKNRNEIKNGTILRLTTSPAQNAQQLHERIQSSSMDAKLEALKDLASLSRDVTFAQEFINLDGISLLTQMVESGTERYQKLQKIMKPCFGDMLSFTLTAFVELMDHGIVSWDTFSVAFIKKIASFVNKSAIDISILQRSLAILESMVLNSHDLYQKVAQEITIGQLIPHLQGTDQEIQTYTIAVINALFLKAPDERRQEMANILAQKQLRYIILTHVIRAQRAINNEMAHQLYVLQVLTFNLLEDRMMTKMDPQDQAQRDIIFELRRIAFDAESEPNNSSGSMEKRKSMYTRDYKKLGFINHVNPAMDFTQTPPGMLALDNMLYFAKHHQDAYIRIVLENSSREDKHECPFGRSSIELTKMLCEILKVGELPSETCNDFHPMFFTHDRSFEEFFCICIQLLNKTWKEMRATSEDFNKVMQVVKEQVMRALTTKPSSLDQFKSKLQNLSYTEILKIRQSERMNQEDFQSRPILELKEKIQPEILELIKQQRLNRLVEGTCFRKLNARRRQDKFWYCRLSPNHKVLHYGDLEESPQGEVPHDSLQDKLPVADIKAVVTGKDCPHMKEKGALKQNKEVLELAFSILYDSNCQLNFIAPDKHEYCIWTDGLNALLGKDMMSDLTRNDLDTLLSMEIKLRLLDLENIQIPDAPPPIPKEPSNYDFVYDCN
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
9UbiquitinationPPPSDIVKVAIEWPG
CCCHHHEEEEEECCC
26.7027667366
18PhosphorylationAIEWPGAYPKLMEID
EEECCCCCCCHHHHC
13.55-
31PhosphorylationIDQKKPLSAIIKEVC
HCCCCCHHHHHHHHH
26.4228833060
59UbiquitinationQHADSSNFYITEKNR
ECCCCCCEEEEECCC
5.1527667366
69UbiquitinationTEKNRNEIKNGTILR
EECCCCCCCCCCEEE
4.8527667366
100AcetylationQSSSMDAKLEALKDL
HHCCHHHHHHHHHHH
42.47-
105AcetylationDAKLEALKDLASLSR
HHHHHHHHHHHHHCC
58.71-
105UbiquitinationDAKLEALKDLASLSR
HHHHHHHHHHHHHCC
58.7127667366
216PhosphorylationVLNSHDLYQKVAQEI
HCCCHHHHHHHHHHC
16.61-
336PhosphorylationRIAFDAESEPNNSSG
HHHHCCCCCCCCCCC
61.1428833060
341PhosphorylationAESEPNNSSGSMEKR
CCCCCCCCCCCCHHH
42.5925521595
342PhosphorylationESEPNNSSGSMEKRK
CCCCCCCCCCCHHHH
36.6926824392
344PhosphorylationEPNNSSGSMEKRKSM
CCCCCCCCCHHHHHH
26.2225521595
350PhosphorylationGSMEKRKSMYTRDYK
CCCHHHHHHHHCCHH
22.5123375375
353PhosphorylationEKRKSMYTRDYKKLG
HHHHHHHHCCHHHHC
14.3929550500
395PhosphorylationAKHHQDAYIRIVLEN
HHHCCCCEEEEEEEC
10.06-
443UbiquitinationETCNDFHPMFFTHDR
CCCCCCCCCCCCCCC
22.6727667366
453UbiquitinationFTHDRSFEEFFCICI
CCCCCCHHHHHHHHH
55.9627667366
511PhosphorylationSKLQNLSYTEILKIR
HHHHCCCHHHHHHHH
16.14-
516UbiquitinationLSYTEILKIRQSERM
CCHHHHHHHHHHHHC
41.31-
539UbiquitinationPILELKEKIQPEILE
CHHHHHHHHCHHHHH
45.0827667366
549UbiquitinationPEILELIKQQRLNRL
HHHHHHHHHHHHHHH
53.6727667366
554UbiquitinationLIKQQRLNRLVEGTC
HHHHHHHHHHHHCCH
37.1127667366
564UbiquitinationVEGTCFRKLNARRRQ
HHCCHHHHHCCCHHC
26.3227667366
588PhosphorylationPNHKVLHYGDLEESP
CCCCEEECCCCCCCC
14.2620415495
594PhosphorylationHYGDLEESPQGEVPH
ECCCCCCCCCCCCCC
17.1022817900
603PhosphorylationQGEVPHDSLQDKLPV
CCCCCCCCHHCCCCH
25.5420415495
618PhosphorylationADIKAVVTGKDCPHM
HHEEEEEECCCCHHH
31.7322817900
622GlutathionylationAVVTGKDCPHMKEKG
EEEECCCCHHHHHCC
2.5824333276
695UbiquitinationTLLSMEIKLRLLDLE
HHHHHHHHHHHHCCC
17.78-
718PhosphorylationPPIPKEPSNYDFVYD
CCCCCCCCCCCCCEE
49.4629899451
720PhosphorylationIPKEPSNYDFVYDCN
CCCCCCCCCCCEECC
18.3329899451
724PhosphorylationPSNYDFVYDCN----
CCCCCCCEECC----
18.1230635358

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
18YPhosphorylationKinaseHCKP08103
Uniprot
216YPhosphorylationKinaseHCKP08103
Uniprot
395YPhosphorylationKinaseHCKP08103
Uniprot
511YPhosphorylationKinaseHCKP08103
Uniprot
720YPhosphorylationKinaseHCKP08103
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELMO1_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 ELMO1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ELMO1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ELMO1_MOUSE

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Related Literatures of Post-Translational Modification

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