EHD3_HUMAN - dbPTM
EHD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EHD3_HUMAN
UniProt AC Q9NZN3
Protein Name EH domain-containing protein 3 {ECO:0000305}
Gene Name EHD3 {ECO:0000312|HGNC:HGNC:3244}
Organism Homo sapiens (Human).
Sequence Length 535
Subcellular Localization Recycling endosome membrane
Peripheral membrane protein
Cytoplasmic side . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cell projection, cilium membrane
Peripheral membrane protein
Cytoplasmic side . Localizes to the cilia
Protein Description ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. [PubMed: 25686250 In vitro causes tubulation of endocytic membranes]
Protein Sequence MFSWLGTDDRRRKDPEVFQTVSEGLKKLYKSKLLPLEEHYRFHEFHSPALEDADFDNKPMVLLVGQYSTGKTTFIRYLLEQDFPGMRIGPEPTTDSFIAVMQGDMEGIIPGNALVVDPKKPFRKLNAFGNAFLNRFVCAQLPNPVLESISVIDTPGILSGEKQRISRGYDFAAVLEWFAERVDRIILLFDAHKLDISDEFSEVIKALKNHEDKMRVVLNKADQIETQQLMRVYGALMWSLGKIVNTPEVIRVYIGSFWSHPLLIPDNRKLFEAEEQDLFRDIQSLPRNAALRKLNDLIKRARLAKVHAYIISSLKKEMPSVFGKDNKKKELVNNLAEIYGRIEREHQISPGDFPNLKRMQDQLQAQDFSKFQPLKSKLLEVVDDMLAHDIAQLMVLVRQEESQRPIQMVKGGAFEGTLHGPFGHGYGEGAGEGIDDAEWVVARDKPMYDEIFYTLSPVDGKITGANAKKEMVRSKLPNSVLGKIWKLADIDKDGMLDDDEFALANHLIKVKLEGHELPNELPAHLLPPSKRKVAE
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
1Acetylation-------MFSWLGTD
-------CCCCCCCC		5.6112665801
3Phosphorylation-----MFSWLGTDDR
-----CCCCCCCCCC		21.7923401153
7Ubiquitination-MFSWLGTDDRRRKD
-CCCCCCCCCCCCCC		32.3422817900
7Phosphorylation-MFSWLGTDDRRRKD
-CCCCCCCCCCCCCC		32.3420873877
32MethylationLKKLYKSKLLPLEEH
HHHHHHCCCCCHHHH		50.30-
40PhosphorylationLLPLEEHYRFHEFHS
CCCHHHHHCHHCCCC		20.46-
69PhosphorylationLLVGQYSTGKTTFIR
EEEEEECCCCHHHHH		37.45-
86UbiquitinationLEQDFPGMRIGPEPT
HHCCCCCCCCCCCCC		2.6224816145
124UbiquitinationDPKKPFRKLNAFGNA
CCCCCCHHCHHHHHH		46.61-
124UbiquitinationDPKKPFRKLNAFGNA
CCCCCCHHCHHHHHH		46.6125015289
162UbiquitinationPGILSGEKQRISRGY
CCCCCCCHHHHCCCC		48.69-
162UbiquitinationPGILSGEKQRISRGY
CCCCCCCHHHHCCCC		48.6923000965
205UbiquitinationDEFSEVIKALKNHED
HHHHHHHHHHHCCHH		53.49-
220UbiquitinationKMRVVLNKADQIETQ
HHHHEECHHHHHHHH		49.5321906983
226PhosphorylationNKADQIETQQLMRVY
CHHHHHHHHHHHHHH		24.2020860994
284PhosphorylationDLFRDIQSLPRNAAL
HHHHHHHHCCHHHHH		40.4530266825
293UbiquitinationPRNAALRKLNDLIKR
CHHHHHHHHHHHHHH		53.12-
299UbiquitinationRKLNDLIKRARLAKV
HHHHHHHHHHHHHHH		47.5029901268
312PhosphorylationKVHAYIISSLKKEMP
HHHHHHHHHHHHHCH		21.7624719451
315SumoylationAYIISSLKKEMPSVF
HHHHHHHHHHCHHHH		48.9426226295
315SumoylationAYIISSLKKEMPSVF
HHHHHHHHHHCHHHH		48.94-
316UbiquitinationYIISSLKKEMPSVFG
HHHHHHHHHCHHHHC		65.62-
339PhosphorylationVNNLAEIYGRIEREH
HHHHHHHHHHHHHHH		7.5821253578
349PhosphorylationIEREHQISPGDFPNL
HHHHHCCCCCCCCCH		19.0924076635
402PhosphorylationVLVRQEESQRPIQMV
HHHHCHHCCCCEEEE		30.6426074081
417PhosphorylationKGGAFEGTLHGPFGH
ECCCCCCEECCCCCC		14.3726074081
453PhosphorylationPMYDEIFYTLSPVDG
CCCCEEEEECCCCCC		16.6626074081
454PhosphorylationMYDEIFYTLSPVDGK
CCCEEEEECCCCCCC		15.2626074081
456PhosphorylationDEIFYTLSPVDGKIT
CEEEEECCCCCCCCC		18.3119413330
463PhosphorylationSPVDGKITGANAKKE
CCCCCCCCCCHHHHH		33.4526074081
475UbiquitinationKKEMVRSKLPNSVLG
HHHHHHCCCCCCHHH		58.35-
479PhosphorylationVRSKLPNSVLGKIWK
HHCCCCCCHHHHHHH		19.4425159151
495SulfoxidationADIDKDGMLDDDEFA
HCCCCCCCCCCHHHH		5.4930846556
511SumoylationANHLIKVKLEGHELP
HHHHEEEEECCCCCC		35.5026226295
511SumoylationANHLIKVKLEGHELP
HHHHEEEEECCCCCC		35.50-
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 EHD3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EHD3_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 EHD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNP29_HUMANSNAP29physical
11423532
EHD1_HUMANEHD1physical
12121420
RBNS5_HUMANRBSNphysical
15020713
RFIP2_HUMANRAB11FIP2physical
16251358
RBNS5_HUMANRBSNphysical
16251358
EHD1_HUMANEHD1physical
16251358
EHD3_HUMANEHD3physical
16251358
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 EHD3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 1-10, AND ACETYLATION AT MET-1.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND MASSSPECTROMETRY.

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