AMFR_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AMFR_MOUSE
• UniProt AC: Q9R049
• Protein Name: E3 ubiquitin-protein ligase AMFR
• Gene Name: Amfr
• Organism: Mus musculus (Mouse).
• Sequence Length: 643
• Subcellular Localization: Endoplasmic reticulum membrane; Multi-pass membrane protein.
• Protein Description: E3 ubiquitin-protein ligase that mediates the polyubiquitination of a number of proteins such as CD3D, CYP3A4, CFTR and APOB for proteasomal degradation. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD). The VCP/p97-AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG complex at the ER membrane and initiating ubiquitination of HMGCR. The ubiquitinated HMGCR is then released from the ER by the complex into the cytosol for subsequent destruction. Also regulates ERAD through the ubiquitination of UBL4A a component of the BAG6/BAT3 complex. Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation. Mediates tumor invasion and metastasis (By similarity)..
• Protein Sequence: MPLLFLERFPWPSLRTYTGLSGLALLGTIVSAYRALSQPEDGSGEPEPLTAPLQPEALAPARLTAGGPRARDVAQYLLSDSLFVWVLVNTACCVLMLVAKLIQCIVFGPLRVSERQHLKDKFWNFIFYKFIFIFGVLNVQTVEEVVMWCLWFAGLVFLHLMVQLCKDRFEYLSFSPTTPMSSHGRVLSLLIAMLLSCCGLAVVCCVTGYTHGMHTLAFMAAESLLVTVRTAHVILRYVIHLWDLNHEGTWEGKGTYVYYTDFVMELALLSLDLMHHIHMLLFGNIWLSMASLVIFMQLRYLFHEVQRRIRRHKNYLRVVGNMEARFAVATPEELAVNNDDCAICWDSMQAARKLPCGHLFHNSCLRSWLEQDTSCPTCRMSLNIADGSRAREDHQGENLDENLVPVAAAEGRPRLNQHNHFFHFDGSRIASWLPSFSVEVMHTTNILGITQASNSQLNAMAHQIQEMFPQVPYHLVLQDLQMTRSVEITTDNILEGRIQVPFPTQRSDSLRPALNSPVERPSPDLEEGEASVQTERVPLDLSPRLEETLDFSEVELEPIEVEDFEARGSRFSKSADERQRMLVQRKDDLLQQARKRFLNKSSEDDGASERLLPSEGTSSDPVTLRRRMLAAAAERRLQRQRTT

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
64	Phosphorylation	ALAPARLTAGGPRAR HHCCCCCCCCCCCHH	20.08	27149854
337	S-palmitoylation	TPEELAVNNDDCAIC CHHHHCCCCCCCCCC	40.37	22728137
340	S-palmitoylation	ELAVNNDDCAICWDS HHCCCCCCCCCCHHH	26.35	22728137
352	S-palmitoylation	WDSMQAARKLPCGHL HHHHHHHHHCCCCCC	44.02	22728137
353	Ubiquitination	DSMQAARKLPCGHLF HHHHHHHHCCCCCCC	52.64	-
360	S-palmitoylation	KLPCGHLFHNSCLRS HCCCCCCCCHHHHHH	4.21	22728137
371	S-palmitoylation	CLRSWLEQDTSCPTC HHHHHHHCCCCCCCC	58.05	22728137
374	S-palmitoylation	SWLEQDTSCPTCRMS HHHHCCCCCCCCEEE	26.79	22728137
507	Phosphorylation	VPFPTQRSDSLRPAL CCCCCCCCCCCCHHH	23.02	21082442
509	Phosphorylation	FPTQRSDSLRPALNS CCCCCCCCCCHHHCC	27.76	27149854
516	Phosphorylation	SLRPALNSPVERPSP CCCHHHCCCCCCCCC	31.04	26643407
522	Phosphorylation	NSPVERPSPDLEEGE CCCCCCCCCCHHCCC	36.95	26239621
531	Phosphorylation	DLEEGEASVQTERVP CHHCCCCCEECEEEC	15.51	26643407
534	Phosphorylation	EGEASVQTERVPLDL CCCCCEECEEECCCC	24.49	26060331
538 (in isoform 2)	Phosphorylation	-	26.78	19144319
542	Phosphorylation	ERVPLDLSPRLEETL EEECCCCCHHHHHCC	13.98	25521595
548	Phosphorylation	LSPRLEETLDFSEVE CCHHHHHCCCCCEEE	23.42	23984901
552	Phosphorylation	LEETLDFSEVELEPI HHHCCCCCEEEEEEE	40.16	30352176
573	Ubiquitination	ARGSRFSKSADERQR HCCCCCCCCHHHHHH	47.12	-
586	Ubiquitination	QRMLVQRKDDLLQQA HHHHHHCHHHHHHHH	38.20	-
600	Ubiquitination	ARKRFLNKSSEDDGA HHHHHHCCCCCCCCC	58.46	-
601	Phosphorylation	RKRFLNKSSEDDGAS HHHHHCCCCCCCCCC	37.58	25159016
602	Phosphorylation	KRFLNKSSEDDGASE HHHHCCCCCCCCCCC	46.80	25159016
608	Phosphorylation	SSEDDGASERLLPSE CCCCCCCCCCCCCCC	28.87	25159016
614	Phosphorylation	ASERLLPSEGTSSDP CCCCCCCCCCCCCCH	48.94	22871156
618	Phosphorylation	LLPSEGTSSDPVTLR CCCCCCCCCCHHHHH	43.53	22871156
619	Phosphorylation	LPSEGTSSDPVTLRR CCCCCCCCCHHHHHH	45.85	22871156

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AMFR_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 AMFR_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TERA_MOUSE	Vcp	physical	16709668
NGLY1_MOUSE	Ngly1	physical	16709668
MGRN1_MOUSE	Mgrn1	physical	26743086

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542, AND MASSSPECTROMETRY.
PubMed: 19144319

"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542, AND MASSSPECTROMETRY.
PubMed: 17114649