ELMO3_HUMAN - dbPTM
ELMO3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELMO3_HUMAN
UniProt AC Q96BJ8
Protein Name Engulfment and cell motility protein 3
Gene Name ELMO3
Organism Homo sapiens (Human).
Sequence Length 720
Subcellular Localization Cytoplasm.
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 MAPPRNVVKIAIKMRDAIPQLIQLDQAKPLAAVLKEVCDAWSLTHSERYALQFADGHRRYITENNRAEIKNGSILCLSTAPDLEAEQLLGGLQSNSPEGRREALRRLVPLASDMIFAREVISRNGLQILGTIIEDGDDLGEVLALSLRAFSELMEHGVVSWETLSIPFVRKVVCYVNMNLMDASVPPLALGLLESVTLSSPALGQLVKSEVPLDRLLVHLQVMNQQLQTKAMALLTALLQGASPVERKHMLDYLWQRNLRQFIYKNIIHSAAPMGDEMAHHLYVLQALMLGLLEPRMRTPLDPYSQEQREQLQVLRQAAFEVEGESSGAGLSADRRRSLCAREFRKLGFSNSNPAQDLERVPPGLLALDNMLYFSRNAPSAYSRFVLENSSREDKHECPFARGSIQLTVLLCELLRVGEPCSETAQDFSPMFFGQDQSFHELFCVGIQLLNKTWKEMRATQEDFDKVMQVVREQLARTLALKPTSLELFRTKVNALTYGEVLRLRQTERLHQEGTLAPPILELREKLKPELMGLIRQQRLLRLCEGTLFRKISSRRRQDKLWFCCLSPNHKLLQYGDMEEGASPPTLESLPEQLPVADMRALLTGKDCPHVREKGSGKQNKDLYELAFSISYDRGEEEAYLNFIAPSKREFYLWTDGLSALLGSPMGSEQTRLDLEQLLTMETKLRLLELENVPIPERPPPVPPPPTNFNFCYDCSIAEP
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
112O-linked_GlycosylationRRLVPLASDMIFARE
HHHHHHHHHHHHHHH		35.0830379171
146PhosphorylationLGEVLALSLRAFSEL
HHHHHHHHHHHHHHH		15.3724719451
233 (in isoform 2)Ubiquitination-12.3221906983
299PhosphorylationLLEPRMRTPLDPYSQ
HCCCCCCCCCCCCCH		20.8929978859
304PhosphorylationMRTPLDPYSQEQREQ
CCCCCCCCCHHHHHH		23.7428152594
305PhosphorylationRTPLDPYSQEQREQL
CCCCCCCCHHHHHHH		32.4028152594
338PhosphorylationLSADRRRSLCAREFR
CCHHHHHHHHHHHHH		26.4524719451
346 (in isoform 1)Ubiquitination-59.2821906983
346UbiquitinationLCAREFRKLGFSNSN
HHHHHHHHCCCCCCC		59.2821906983
352PhosphorylationRKLGFSNSNPAQDLE
HHCCCCCCCHHHHHH		42.8828857561
380O-linked_GlycosylationYFSRNAPSAYSRFVL
ECCCCCCCHHHHHHH		37.1130379171
391PhosphorylationRFVLENSSREDKHEC
HHHHCCCCCCCCCCC		51.8024719451
399 (in isoform 3)Ubiquitination-23.9721906983
399UbiquitinationREDKHECPFARGSIQ
CCCCCCCCCCCHHHH		23.97-
453PhosphorylationGIQLLNKTWKEMRAT
HHHHHHHHHHHHHHC		40.4729759185
460PhosphorylationTWKEMRATQEDFDKV
HHHHHHHCHHHHHHH		23.3329759185
497PhosphorylationRTKVNALTYGEVLRL
HHHHHHCHHHHHHHH		27.3728442448
498PhosphorylationTKVNALTYGEVLRLR
HHHHHCHHHHHHHHH		16.4928152594
508UbiquitinationVLRLRQTERLHQEGT
HHHHHHHHHHHHCCC		44.93-
551PhosphorylationCEGTLFRKISSRRRQ
HHCCHHHHHCCCCCC		39.34-
571 (in isoform 2)Ubiquitination-58.4921906983
575PhosphorylationPNHKLLQYGDMEEGA
CCCCEECCCCCCCCC		18.3130624053
583PhosphorylationGDMEEGASPPTLESL
CCCCCCCCCCCHHHC		42.1226657352
586PhosphorylationEEGASPPTLESLPEQ
CCCCCCCCHHHCCCC		46.6830624053
589PhosphorylationASPPTLESLPEQLPV
CCCCCHHHCCCCCCH		52.9530624053
636PhosphorylationSISYDRGEEEAYLNF
EEEECCCCCEEHHEE		54.2624719451
680PhosphorylationLDLEQLLTMETKLRL
CCHHHHHHHHHHHHH		22.8923403867
684 (in isoform 1)Ubiquitination-20.5021906983
684UbiquitinationQLLTMETKLRLLELE
HHHHHHHHHHHHHHC		20.502190698
737Ubiquitination------------------------
------------------------		-
737 (in isoform 3)Ubiquitination-21906983
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 ELMO3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELMO3_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 ELMO3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARL4A_HUMANARL4Aphysical
21930703
DOCK1_HUMANDOCK1physical
28514442
DOCK3_HUMANDOCK3physical
28514442
DOCK5_HUMANDOCK5physical
28514442
DOCK4_HUMANDOCK4physical
28514442
ELMO2_HUMANELMO2physical
28514442
ELMO1_HUMANELMO1physical
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 ELMO3_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-498, AND MASSSPECTROMETRY.

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