EHD2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EHD2_MOUSE
• UniProt AC: Q8BH64
• Protein Name: EH domain-containing protein 2 {ECO:0000305}
• Gene Name: Ehd2 {ECO:0000312|MGI:MGI:2154274}
• Organism: Mus musculus (Mouse).
• Sequence Length: 543
• Subcellular Localization: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side . Membrane, caveola ; Peripheral membrane protein ; Cytoplasmic side . Endosome membrane ; Peripheral membrane protein ; Cytoplasmic side . Cytoplasm, cytosol . Colocalizes with GLUT4 in
• Protein Description: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. [PubMed: 24508342 Plays a role in membrane trafficking between the plasma membrane and endosomes. Important for the internalization of GLUT4]
• Protein Sequence: MFSWLKKGGARGQRPEAIRTVTSSLKELYRTKLLPLEEHYRFGSFHSPALEDADFDGKPMVLVAGQYSTGKTSFIQYLLEQEVPGSRVGPEPTTDCFVAVMHGETEGTVPGNALVVDPEKPFRKLNPFGNTFLNRFMCAQLPNQVLESISIIDTPGILSGAKQRVSRGYDFPAVLRWFAERVDLIILLFDAHKLEISDEFSEAIGALRGHEDKIRVVLNKADMVETQQLMRVYGALMWALGKVVGTPEVLRVYIGSFWSQPLLVPDNRRLFELEEQDLFRDIQGLPRHAALRKLNDLVKRARLVRVHAYIISYLKKEMPTVFGKENKKKQLILKLPVIFAKIQLEHHISPGDFPDCQKMQELLMAHDFTKFHSLKPKLLEALDDMLAQDIAKLMPLLRQEELESVEAGVQGGAFEGTRMGPFVERGPDEAIEDGEEGSEDDAEWVVTKDKSKYDEIFYNLAPADGKLSGSKAKTWMVGTKLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEAKLEGHGLPTNLPRRLVPPSKRRQKGSAE

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
3	Phosphorylation	-----MFSWLKKGGA -----CCCCCCCCCC	30.15	-
6	Ubiquitination	--MFSWLKKGGARGQ --CCCCCCCCCCCCC	43.01	22790023
11	Methylation	WLKKGGARGQRPEAI CCCCCCCCCCCHHHH	45.08	-
22	Phosphorylation	PEAIRTVTSSLKELY HHHHHHHHHHHHHHH	16.40	30482847
23	Phosphorylation	EAIRTVTSSLKELYR HHHHHHHHHHHHHHH	29.36	22817900
24	Phosphorylation	AIRTVTSSLKELYRT HHHHHHHHHHHHHHC	33.81	30482847
44	Phosphorylation	EEHYRFGSFHSPALE HHHHCCCCCCCCCCC	19.64	27180971
47	Phosphorylation	YRFGSFHSPALEDAD HCCCCCCCCCCCCCC	15.17	21082442
58	Ubiquitination	EDADFDGKPMVLVAG CCCCCCCCEEEEEEE	31.61	22790023
124	Ubiquitination	DPEKPFRKLNPFGNT CCCCCCCCCCCCCCH	53.66	22790023
138	S-nitrosocysteine	TFLNRFMCAQLPNQV HHHHHHHHHHCCHHH	1.69	-
138	S-nitrosylation	TFLNRFMCAQLPNQV HHHHHHHHHHCCHHH	1.69	21278135
324	Acetylation	EMPTVFGKENKKKQL HCCCCCCCCCCCEEE	46.80	7611795
349	Phosphorylation	IQLEHHISPGDFPDC HHHHCCCCCCCCCCH	20.62	-
356	S-nitrosocysteine	SPGDFPDCQKMQELL CCCCCCCHHHHHHHH	4.22	-
356	S-nitrosylation	SPGDFPDCQKMQELL CCCCCCCHHHHHHHH	4.22	21278135
369	Phosphorylation	LLMAHDFTKFHSLKP HHHHCCHHHHHCCCH	38.57	29899451
373	Phosphorylation	HDFTKFHSLKPKLLE CCHHHHHCCCHHHHH	41.02	26824392
438	Phosphorylation	IEDGEEGSEDDAEWV CCCCCCCCCCCCCEE	40.92	24925903
447	Phosphorylation	DDAEWVVTKDKSKYD CCCCEEEECCHHHCC	24.73	25619855
451	Phosphorylation	WVVTKDKSKYDEIFY EEEECCHHHCCCHHH	46.73	25619855
452	Acetylation	VVTKDKSKYDEIFYN EEECCHHHCCCHHHC	63.56	23806337
452	Ubiquitination	VVTKDKSKYDEIFYN EEECCHHHCCCHHHC	63.56	22790023
453	Phosphorylation	VTKDKSKYDEIFYNL EECCHHHCCCHHHCC	26.37	25619855
458	Phosphorylation	SKYDEIFYNLAPADG HHCCCHHHCCCCCCC	18.22	25619855
466	Ubiquitination	NLAPADGKLSGSKAK CCCCCCCCCCCCCCC	39.77	22790023
468	Phosphorylation	APADGKLSGSKAKTW CCCCCCCCCCCCCCE	44.50	25521595
470	Phosphorylation	ADGKLSGSKAKTWMV CCCCCCCCCCCCEEC	26.51	25521595
473	Ubiquitination	KLSGSKAKTWMVGTK CCCCCCCCCEECCCC	46.59	22790023
474	Phosphorylation	LSGSKAKTWMVGTKL CCCCCCCCEECCCCC	24.53	23684622
480	Ubiquitination	KTWMVGTKLPNSVLG CCEECCCCCCCCHHH	56.89	22790023
484	Phosphorylation	VGTKLPNSVLGRIWK CCCCCCCCHHHHHHH	19.44	27180971
493	Phosphorylation	LGRIWKLSDVDRDGM HHHHHHHHCCCCCCC	31.68	23608596
524	Phosphorylation	LEGHGLPTNLPRRLV HCCCCCCCCCCCCCC	55.20	26824392

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

Oops, there are no upstream regulatory protein records of EHD2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EHD2_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 EHD2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of EHD2_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASSSPECTROMETRY.
PubMed: 19131326

"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-468, AND MASSSPECTROMETRY.
PubMed: 19367708

"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASSSPECTROMETRY.
PubMed: 15345747