ECM29_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ECM29_MOUSE
• UniProt AC: Q6PDI5
• Protein Name: Proteasome adapter and scaffold protein ECM29 {ECO:0000250|UniProtKB:Q5VYK3}
• Gene Name: Ecpas
• Organism: Mus musculus (Mouse).
• Sequence Length: 1840
• Subcellular Localization: Endoplasmic reticulum . Endoplasmic reticulum-Golgi intermediate compartment . Endosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Nucleus . Endosome, multivesicular body . Cytoplasmic vesicle .
• Protein Description: Adapter/scaffolding protein that binds to the 26S proteasome, motor proteins and other compartment specific proteins. May couple the proteasome to different compartments including endosome, endoplasmic reticulum and centrosome. May play a role in ERAD and other enhanced proteolyis (By similarity). Promotes proteasome dissociation under oxidative stress. [PubMed: 26802743]
• Protein Sequence: METGSDSDQLERVFLRLGHAETDEQLQNIISKFLPPVLLKLSSTQEGVRKKVMELLVHLNKRIKSRPKIQLPVETLLVQYQDPAAVSFVTNFTIIYVKMGYPRLPVEKQCELAPTLLTAMEGKPQPQQDSLMHLLIPTLFHMKYPAESSKSASPFNLAEKPKTVQLLLDFMLDVLLMPYGYVLNESQSRQNSSSSSQGSSSNSGGGSGIPQPPPGMSFYAAKRVIGDNPWTPEQLEQCKLGIVKFIEAEQVPELEAVLHLVIASSDTRHSVATAADLELKSKQSLIDWNNPAIINKMYKVYLGDIPLKTKEGAVLKPELKRDPVSTRVKLKIVPHLLRSRQAAETFPANIQVVYDGLFGTNTNSKLRTLSLQFVHHICLTCPEIKIKPLGPMLLNGLTKLINEYKEDPKLLSMAYSAVGKLSSRMPHLFTKDIALVQQLFEALCKEEPETRLAIQEALSMMVGAYSTLEGAQRTLMEALVASYLIKPEVQVRQVAVKFASTVFPSDHIPSRYLLLLAAGDPREEVHGEAQRVLRCLPGRNKKESASKQMPSFPEMVYYIQEKASHRMKTPVKYMTGTTVLPFNPAAFGEIVLYLRMCLAHSAGVVPTSQSLADMQDHAPAIGRYIRALMSSSQATASSSNKSGETNPVQIYTGLLQQLLAGVGGLPVMYCLLEAVSVYPEKLATKFVDKTEWIKSLMSSSKEEMRELAALFYSVVVSTVSGIELKSMIEQLIKATKDNHSPEVQHGSLLALGFTVGRYLAKKRVRMAEQHDLETDADLLPEQEEIIRSATETIGSFLDSTSPLLAIAACTALGEIGRNGPLPIPSEGSGFTKLHLVESLLNRIPSSKETNKMKERAIQTLGYFPVGDGVFPHQKLLLQGLMDSVEAKQIELQFTIGEAITSAAIGTNSVAARDAWLVTEEEYIPPAGAKVNDVVPWVLDVILNKHIISPNPHVRQAACIWLLSLVRKLSTHREVKSHLKEIQSAFVSVLSENDELSQDVASKGLGLVYELGNEQDQQELVSTLVETLMTGKRVKHEVSGETVVFQGGGLGKTPDGQGLSTYKELCSLASDLSQPDLVYKFMNLANHHAMWNSRKGAAFGFNVIATRAGEQLAPFLPQLVPRLYRYQFDPNLGIRQAMTSIWNALVTDKSMVDKYLKEILQDLIKNLTSNMWRVRESSCLALNDLLRGRPLDDVIDKLPEMWETLFRVQDDIKESVRKAAELALKTLSKVCVKMCDPAKGAAGQRTIAVLLPCLLDKGMMSPVTEVRALSINTLVKISKSAGAMLKPHAPKLIPALLESLSVLEPQVLNYLSLRATEQEKDVMDSARLSAAKSSPMMETINMCLQYLDVSVLGELVPRLCELIRSGVGLGTKGGCASVIVSLTTQCPQDLTPYSGKLMSALLSGLTDRNSVIQKSCAFAMGHLVRTSRDSSTEKLLQKLNGWYMEKDEPVYKTSCALTIHAIGRYSPDVLKNHAKEVLPLAFLGMHEIADEEKSEKEECNMWTEVWQENVPGSFGGIRLYLQELITITQKALQSQSWKMKAQGAIAMASISKQTSSLVPPYLGMILSALMQGLAGRTWAGKEELLKAIACVVTACSTELEKSVPNQPTTNEILQAVLKECCKENLKYKIVAISCAADVLKATKEDRFQEFSDIVIPLIKKNSLESMGVRTTKAEDENEKERELQLESLLGAFESLGKAWPRNPDTQRCYRQELCKLMCERLRLSTWKVQLGVLQSMNAFFQGLMLLEEEHADPEALAEILLETCKSITYSLENKTYSSVRTEALSVVELLLKKLEEAKQWESLTAECRGLLIESLATMETDNRPELQEKASVLKKTLESLE

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
40	Ubiquitination	FLPPVLLKLSSTQEG HHCHHHHHCCCCCHH	42.01	22790023
98	Ubiquitination	NFTIIYVKMGYPRLP CEEEEEEECCCCCCC	15.05	27667366
140	Ubiquitination	HLLIPTLFHMKYPAE HHHHHHHHCCCCCCC	6.10	27667366
142	Ubiquitination	LIPTLFHMKYPAESS HHHHHHCCCCCCCCC	3.31	27667366
148	Ubiquitination	HMKYPAESSKSASPF CCCCCCCCCCCCCCC	45.21	27667366
150	Ubiquitination	KYPAESSKSASPFNL CCCCCCCCCCCCCCC	60.36	22790023
156	Ubiquitination	SKSASPFNLAEKPKT CCCCCCCCCCCCCHH	41.55	27667366
256	Ubiquitination	EQVPELEAVLHLVIA HHCCCHHHHHHHHHC	23.07	27667366
258	Ubiquitination	VPELEAVLHLVIASS CCCHHHHHHHHHCCC	3.13	27667366
264	Ubiquitination	VLHLVIASSDTRHSV HHHHHHCCCCCCCCH	20.02	27667366
280	Ubiquitination	TAADLELKSKQSLID HHHCHHCCCCCCCCC	46.35	22790023
308	Ubiquitination	YLGDIPLKTKEGAVL HHCCCCCCCCCCCCC	52.80	22790023
310	Ubiquitination	GDIPLKTKEGAVLKP CCCCCCCCCCCCCCH	53.19	22790023
314	Ubiquitination	LKTKEGAVLKPELKR CCCCCCCCCCHHHCC	11.82	27667366
316	Ubiquitination	TKEGAVLKPELKRDP CCCCCCCCHHHCCCC	29.82	27667366
322	Ubiquitination	LKPELKRDPVSTRVK CCHHHCCCCCCHHHH	46.49	27667366
325	Phosphorylation	ELKRDPVSTRVKLKI HHCCCCCCHHHHHHH	18.84	21659605
326	Phosphorylation	LKRDPVSTRVKLKIV HCCCCCCHHHHHHHH	39.45	-
387	Ubiquitination	TCPEIKIKPLGPMLL CCCCCCCCCCCHHHH	29.23	22790023
547	Acetylation	NKKESASKQMPSFPE CCCCCHHHCCCCCHH	50.78	23236377
712	Phosphorylation	RELAALFYSVVVSTV HHHHHHHHHHHHHHC	11.04	28059163
713	Phosphorylation	ELAALFYSVVVSTVS HHHHHHHHHHHHHCC	10.91	28059163
735	Phosphorylation	IEQLIKATKDNHSPE HHHHHHHHCCCCCCC	33.65	-
740	Phosphorylation	KATKDNHSPEVQHGS HHHCCCCCCCCCCCC	29.07	-
825	Phosphorylation	NGPLPIPSEGSGFTK CCCCCCCCCCCCCHH	56.14	29233185
828	Phosphorylation	LPIPSEGSGFTKLHL CCCCCCCCCCHHHHH	27.04	25338131
831	Phosphorylation	PSEGSGFTKLHLVES CCCCCCCHHHHHHHH	35.90	29514104
1038	Phosphorylation	KRVKHEVSGETVVFQ CCEEEEECCCEEEEE	28.11	25338131
1041	Phosphorylation	KHEVSGETVVFQGGG EEEECCCEEEEECCC	26.04	25338131
1232	Malonylation	TLSKVCVKMCDPAKG HHHHHHHHHCCCCCC	28.78	26320211
1409	Phosphorylation	SGLTDRNSVIQKSCA HCCCCCCHHHHHHHH	22.84	29514104
1433	Malonylation	SRDSSTEKLLQKLNG CCCCHHHHHHHHHCC	55.36	26320211
1437	Malonylation	STEKLLQKLNGWYME HHHHHHHHHCCCHHC	43.84	26320211
1437	Acetylation	STEKLLQKLNGWYME HHHHHHHHHCCCHHC	43.84	23236377
1661	Phosphorylation	IPLIKKNSLESMGVR HHHHHHCCHHHCCCC	42.25	29176673

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

Oops, there are no upstream regulatory protein records of ECM29_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ECM29_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 ECM29_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANXA2_HUMAN	ANXA2	physical	26496610
RPA34_HUMAN	CD3EAP	physical	26496610
COBL1_HUMAN	COBLL1	physical	26496610
PHF3_HUMAN	PHF3	physical	26496610
PHAR4_HUMAN	PHACTR4	physical	26496610

Drug and Disease Associations

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