EHD3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EHD3_MOUSE
• UniProt AC: Q9QXY6
• Protein Name: EH domain-containing protein 3 {ECO:0000305}
• Gene Name: Ehd3 {ECO:0000312|MGI:MGI:1928900}
• Organism: Mus musculus (Mouse).
• 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 . Cytoplasmic vesicle .
• Protein Description: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. In vitro causes tubulation of endocytic membranes (By similarity). Binding to phosphatidic acid induces its membrane tubulation activity. [PubMed: 26896729 Plays a role in endocytic transport. Involved in early endosome to recycling endosome compartment (ERC), retrograde early endosome to Golgi, and endosome to plasma membrane (rapid recycling) protein transport. Involved in the regulation of Golgi maintenance and morphology (By similarity Involved in the recycling of internalized D1 dopamine receptor (By similarity Plays a role in cardiac protein trafficking probably implicating ANK2. Involved in the ventricular membrane targeting of SLC8A1 and CACNA1C and probably the atrial membrane localization of CACNA1GG and CACNA1H implicated in the regulation of atrial myocyte excitability and cardiac conduction]
• Protein Sequence: MFSWLGNDDRRKKDPEVFQTVSDGLKKLYKTKLLPLEEYYRFHEFHSPALEDADFDNKPMVLLVGQYSTGKTTFIRYLLEQDFPGMRIGPEPTTDSFIAVMQGDVEGIIPGNALVVDPKKPFRKLNAFGNAFLNRFVCAQLPNAVLESISVIDTPGILSGEKQRISRGYDFAAVLEWFAERVDRIILLFDAHKLDISDEFSEVIKALKNHEDKMRVVLNKADQIETQQLMRVYGALMWSLGKIVNTPEVIRVYIGSFWSHPLLIPDNRKLFEAEEQDLFRDIQSLPRNAALRKLNDLIKRARLAKVHAYIISSLKKEMPSVFGKDTKKKELVNNLAEIYGRIEREHQISPGDFPNLKRMQDQLQAQDFSKFQPLKSKLLEVVDDMLAHDIAQLMVLVRQEETQRPVQMVKGGAFEGTLQGPFGHGYGEGAGEGIDDAEWVVARDKPMYDEIFYTLSPVDGKITGANAKKEMVRSKLPNSVLGKIWKLADIDKDGMLDDEEFALANHLIKVKLEGHELPSELPAHLLPPSKRKVSE

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
1	Acetylation	-------MFSWLGND -------CCCCCCCC	5.61	-
13	Ubiquitination	GNDDRRKKDPEVFQT CCCCHHCCCHHHHHH	76.37	22790023
26	Ubiquitination	QTVSDGLKKLYKTKL HHHHHHHHHHHCCCC	46.38	22790023
32	Ubiquitination	LKKLYKTKLLPLEEY HHHHHCCCCCCHHHH	43.82	22790023
39	Phosphorylation	KLLPLEEYYRFHEFH CCCCHHHHHHHHHCC	7.20	20531401
40	Phosphorylation	LLPLEEYYRFHEFHS CCCHHHHHHHHHCCC	15.30	20531401
47	Phosphorylation	YRFHEFHSPALEDAD HHHHHCCCCCCCCCC	19.72	22324799
58	Ubiquitination	EDADFDNKPMVLLVG CCCCCCCCCEEEEEE	36.01	-
124	Ubiquitination	DPKKPFRKLNAFGNA CCCCCCHHCHHHHHH	46.61	27667366
162	Ubiquitination	PGILSGEKQRISRGY CCCCCCCHHHHCCCC	48.69	27667366
205	Ubiquitination	DEFSEVIKALKNHED HHHHHHHHHHHCCHH	53.49	-
220	Ubiquitination	KMRVVLNKADQIETQ HHHHEECHHHHHHHH	49.53	-
269	Ubiquitination	LLIPDNRKLFEAEEQ EECCCCHHHHHHHHH	64.88	22790023
284	Phosphorylation	DLFRDIQSLPRNAAL HHHHHHHHCCHHHHH	40.45	29472430
293	Ubiquitination	PRNAALRKLNDLIKR CHHHHHHHHHHHHHH	53.12	-
299	Ubiquitination	RKLNDLIKRARLAKV HHHHHHHHHHHHHHH	47.50	27667366
299	Acetylation	RKLNDLIKRARLAKV HHHHHHHHHHHHHHH	47.50	7614641
349	Phosphorylation	IEREHQISPGDFPNL HHHHHCCCCCCCCCH	19.09	25521595
357	Ubiquitination	PGDFPNLKRMQDQLQ CCCCCCHHHHHHHHH	53.09	22790023
370	Ubiquitination	LQAQDFSKFQPLKSK HHHCCHHHCCCHHHH	48.27	22790023
410	Ubiquitination	QRPVQMVKGGAFEGT CCCEEEEECCCCCCC	46.41	22790023
453	Phosphorylation	PMYDEIFYTLSPVDG CCCCEEEEECCCCCC	16.66	22817900
454	Phosphorylation	MYDEIFYTLSPVDGK CCCEEEEECCCCCCC	15.26	29899451
456	Phosphorylation	DEIFYTLSPVDGKIT CEEEEECCCCCCCCC	18.31	25521595
475	Ubiquitination	KKEMVRSKLPNSVLG HHHHHHCCCCCCHHH	58.35	22790023
479	Phosphorylation	VRSKLPNSVLGKIWK HHCCCCCCHHHHHHH	19.44	22942356
483	Ubiquitination	LPNSVLGKIWKLADI CCCCHHHHHHHHHCC	41.03	22790023

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of EHD3_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EHD3_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of EHD3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EHD3_MOUSE	Ehd3	physical	12121420
EHD1_HUMAN	EHD1	physical	12121420

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND MASSSPECTROMETRY.
PubMed: 19367708