ERAP1_HUMAN - dbPTM
ERAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERAP1_HUMAN
UniProt AC Q9NZ08
Protein Name Endoplasmic reticulum aminopeptidase 1
Gene Name ERAP1
Organism Homo sapiens (Human).
Sequence Length 941
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..
Protein Sequence MVFLPLKWSLATMSFLLSSLLALLTVSTPSWCQSTEASPKRSDGTPFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMASICPTDGVKGMDGFCSRSQHSSSSSHWHQEGVDVKTMMNTWTLQKGFPLITITVRGRNVHMKQEHYMKGSDGAPDTGYLWHVPLTFITSKSDMVHRFLLKTKTDVLILPEEVEWIKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYLKHETEIMPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPCVQRAEGYFRKWKESNGNLSLPVDVTLAVFAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQEFPQILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQLRCVQQTIETIEENIGWMDKNFDKIRVWLQSEKLERM
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 Orthologous
Protein Cluster
9PhosphorylationVFLPLKWSLATMSFL
CCCCCCHHHHHHHHH		13.4121406692
12PhosphorylationPLKWSLATMSFLLSS
CCCHHHHHHHHHHHH		20.7421406692
12 (in isoform 2)Phosphorylation-20.7421406692
14 (in isoform 2)Phosphorylation-14.3721406692
14PhosphorylationKWSLATMSFLLSSLL
CHHHHHHHHHHHHHH		14.3721406692
18PhosphorylationATMSFLLSSLLALLT
HHHHHHHHHHHHHHH		22.5321406692
19PhosphorylationTMSFLLSSLLALLTV
HHHHHHHHHHHHHHC		27.6321406692
25PhosphorylationSSLLALLTVSTPSWC
HHHHHHHHCCCCHHH		17.1721406692
27PhosphorylationLLALLTVSTPSWCQS
HHHHHHCCCCHHHHC		29.3921406692
28PhosphorylationLALLTVSTPSWCQST
HHHHHCCCCHHHHCC		19.6021406692
30 (in isoform 2)Phosphorylation-40.3421406692
30PhosphorylationLLTVSTPSWCQSTEA
HHHCCCCHHHHCCCC		40.3421406692
34PhosphorylationSTPSWCQSTEASPKR
CCCHHHHCCCCCCCC		25.6921406692
35PhosphorylationTPSWCQSTEASPKRS
CCHHHHCCCCCCCCC		15.0821406692
38PhosphorylationWCQSTEASPKRSDGT
HHHCCCCCCCCCCCC		25.4021406692
70N-linked_GlycosylationYDLLIHANLTTLTFW
HHEEEECCCCEEEEE		24.6121478864
154N-linked_GlycosylationVVIHYAGNLSETFHG
EEEEECCCHHHHCCE		32.0221478864
179 (in isoform 2)Phosphorylation-21.2121406692
179PhosphorylationGELRILASTQFEPTA
CEEEEEEEECCCCCC		21.2120068231
180PhosphorylationELRILASTQFEPTAA
EEEEEEEECCCCCCH		31.5021406692
185 (in isoform 2)Phosphorylation-26.2521406692
185PhosphorylationASTQFEPTAARMAFP
EEECCCCCCHHHHCC		26.2520068231
202PhosphorylationDEPAFKASFSIKIRR
CCCCCEEEEEEEECC		21.8124719451
204PhosphorylationPAFKASFSIKIRREP
CCCEEEEEEEECCCC		22.0724719451
268 (in isoform 2)Phosphorylation-12.0527251275
268PhosphorylationTKSGVKVSVYAVPDK
HCCCCEEEEEECCCC		12.0527251275
270PhosphorylationSGVKVSVYAVPDKIN
CCCEEEEEECCCCCC		8.38-
399PhosphorylationPELKVGDYFFGKCFD
CCCCCCCEECCCCCC		8.5520068231
414N-linked_GlycosylationAMEVDALNSSHPVST
EEEHHHCCCCCCCCC		43.0919159218
432SulfoxidationNPAQIREMFDDVSYD
CHHHHHHHHHCCCCC		2.9930846556
440 (in isoform 2)Ubiquitination-39.93-
440UbiquitinationFDDVSYDKGACILNM
HHCCCCCHHHHHHHH		39.93-
451PhosphorylationILNMLREYLSADAFK
HHHHHHHHHCHHHHH		10.26-
458UbiquitinationYLSADAFKSGIVQYL
HHCHHHHHHHHHHHH		49.87-
458 (in isoform 2)Ubiquitination-49.87-
464PhosphorylationFKSGIVQYLQKHSYK
HHHHHHHHHHHCCCC		10.54-
473PhosphorylationQKHSYKNTKNEDLWD
HHCCCCCCCCHHHHH		30.9720068231
481PhosphorylationKNEDLWDSMASICPT
CCHHHHHHHHHHCCC		12.5020068231
484PhosphorylationDLWDSMASICPTDGV
HHHHHHHHHCCCCCC		18.9720068231
488PhosphorylationSMASICPTDGVKGMD
HHHHHCCCCCCCCCC		40.7620068231
499PhosphorylationKGMDGFCSRSQHSSS
CCCCCCCCCCCCCCC		32.4820068231
505O-linked_GlycosylationCSRSQHSSSSSHWHQ
CCCCCCCCCCCCHHH		31.92OGP
507O-linked_GlycosylationRSQHSSSSSHWHQEG
CCCCCCCCCCHHHCC		28.33OGP
508O-linked_GlycosylationSQHSSSSSHWHQEGV
CCCCCCCCCHHHCCC		32.32OGP
550SulfoxidationHMKQEHYMKGSDGAP
CCCHHHCCCCCCCCC		4.2330846556
559PhosphorylationGSDGAPDTGYLWHVP
CCCCCCCCCCEEEEE		27.02-
608PhosphorylationNVGMNGYYIVHYEDD
ECCCCCEEEEEEECC		9.6217384208
692SulfoxidationKLMEKRDMNEVETQF
HHHHHCCHHHHHHHH		5.5221406390
760N-linked_GlycosylationKWKESNGNLSLPVDV
HHHHHCCCCCCCCEE		30.6121478864
811AcetylationALCRTQNKEKLQWLL
EEECCCCHHHHHHHH		46.547710561
868PhosphorylationVQKFELGSSSIAHMV
HHHHCCCCCHHHHHH		33.2723663014
869PhosphorylationQKFELGSSSIAHMVM
HHHCCCCCHHHHHHH		24.7823663014
870PhosphorylationKFELGSSSIAHMVMG
HHCCCCCHHHHHHHC		26.0323663014
879PhosphorylationAHMVMGTTNQFSTRT
HHHHHCCCCCCCCHH		22.6923532336
883PhosphorylationMGTTNQFSTRTRLEE
HCCCCCCCCHHHHHH		13.7623532336
901N-linked_GlycosylationFFSSLKENGSQLRCV
HHHHHHHCCHHHHHH		54.55UniProtKB CARBOHYD
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of ERAP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERAP1_HUMAN !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ERAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MUL1_HUMANMUL1physical
28514442
TM87A_HUMANTMEM87Aphysical
28514442
APOL2_HUMANAPOL2physical
28514442
MOT10_HUMANSLC16A10physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERAP1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural basis for antigenic peptide precursor processing by theendoplasmic reticulum aminopeptidase ERAP1.";
Nguyen T.T., Chang S.C., Evnouchidou I., York I.A., Zikos C.,Rock K.L., Goldberg A.L., Stratikos E., Stern L.J.;
Nat. Struct. Mol. Biol. 18:604-613(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 37-939 IN COMPLEX WITH ZINCIONS AND BESTATIN, FUNCTION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-70;ASN-154 AND ASN-760, ACTIVE SITE, CATALYTIC ACTIVITY, SUBUNIT, ANDMUTAGENESIS OF TYR-438.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-414, AND MASSSPECTROMETRY.

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