ERAP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ERAP1_MOUSE
• UniProt AC: Q9EQH2
• Protein Name: Endoplasmic reticulum aminopeptidase 1
• Gene Name: Erap1
• Organism: Mus musculus (Mouse).
• Sequence Length: 930
• Subcellular Localization: Endoplasmic reticulum membrane; Single-pass type II membrane protein.
• Protein Description: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney (By similarity)..
• Protein Sequence: MPSLLPLVLTFLSVSSPSWCQNSDIESLKASNGDSFPWNNMRLPEYMTPIHYDLMIHANLSTLTFWGKTEVEIIASRPTSTIIMHSHHLQISKATLRRGAGEMLSEEPLKVLEYPAHEQVALLAAQPLLAGSLYTVIIDYAANLSESFHGFYKSTYRTQEGEMRILAATQFEPTAARMAFPCFDEPALKASFSIKIKRDPRHLAISNMPLVKSVNVAEGLIEDHFDITVKMSTYLVAFIISDFKSVSKMTKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFNIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESSLLYDKEKSSASSKLGITMIVSHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVTVTHPELKVEDYFFGKCFNAMEVDALNSSHPVSTPVENPAQIREMFDDVSYEKGACILNMLRDYLSADTFKRGIVQYLQKYSYKNTKNEDLWNSMMHICPTDGTQTMDGFCSRSQHSSSTSHWRQEVVDVKTMMNTWTLQKGFPLITITVSGRNVHMKQEHYMKGSERFPETGYLWHVPLTFITSKSDSVQRFLLKTKTDVLILPEAVQWIKFNVGMNGYYIVHYADDGWASLSGLLKEAHTTISSNDRASLINNAFQLVSIEKLSIEKALDLTLYLKNETEIMPIFQALNELIPMYKLMEKRDMIEVETQFKDFLLKLLKDLIDKQTWTDEGSVSERMLRSQLLLLACVRNYQPCVQRAERYFREWKSSNGNMSIPIDVTLAVFAVGAQNTEGWDFLYSKYQSSLSSTEKSQIEFSLCTSKDPEKLQWLLDQSFKGEIIKTQEFPHILTLIGRNPVGYPLAWKFLRENWNKLVQKFELGSSSIAHMVMGTTDQFSTRARLEEVKGFFSSLKENGSQLRCVQQTIETIEENIRWMDKNFDKIRLWLQKEKPELL

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
59	N-linked_Glycosylation	YDLMIHANLSTLTFW HHEEEEEECCCEEEC	21.99	-
143	N-linked_Glycosylation	VIIDYAANLSESFHG HHHHHHHHCCHHHCC	35.61	-
182	S-palmitoylation	AARMAFPCFDEPALK HHHHHCCCCCCCCCC	5.61	28526873
206	Phosphorylation	DPRHLAISNMPLVKS CCCCEEECCCCCCCE	22.82	-
403	N-linked_Glycosylation	AMEVDALNSSHPVST CEEHHHCCCCCCCCC	43.09	-
432	S-palmitoylation	VSYEKGACILNMLRD CCHHHHHHHHHHHHH	5.05	28526873
508	Phosphorylation	QEVVDVKTMMNTWTL HHHHHHHHHHHHCCC	22.85	28576409
655	N-linked_Glycosylation	DLTLYLKNETEIMPI HHEEECCCCCCHHHH	59.85	-
749	N-linked_Glycosylation	EWKSSNGNMSIPIDV HHHHCCCCCCCCCEE	25.86	-
888	Ubiquitination	KGFFSSLKENGSQLR HHHHHHHHHCCHHHH	51.59	22790023
890	N-linked_Glycosylation	FFSSLKENGSQLRCV HHHHHHHCCHHHHHH	54.55	-

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

Oops, there are no upstream regulatory protein records of ERAP1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ERAP1_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 ERAP1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ERAP1_MOUSE !!

Drug and Disease Associations

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