ERAP2_HUMAN - dbPTM
ERAP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERAP2_HUMAN
UniProt AC Q6P179
Protein Name Endoplasmic reticulum aminopeptidase 2
Gene Name ERAP2
Organism Homo sapiens (Human).
Sequence Length 960
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. Preferentially hydrolyzes the basic residues Arg and Lys..
Protein Sequence MFHSSAMVNSHRKPMFNIHRGFYCLTAILPQICICSQFSVPSSYHFTEDPGAFPVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSNATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVPEKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHFETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQASLKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDPKTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLKEGFAKYMELIAVNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEVSYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNSCLESDFTSGGVCHSDPKMTSNMLAFLGENAEVKEMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGVFQEDPEWRALQERYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSNGYYIVHYEGHGWDQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKALDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISENLKRYLLQYFKPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMESSGKLNIPTDVLKIVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYALSTSKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENWTHLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDIFQTVLETITKNIKWLEKNLPTLRTWLMVNT
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
39O-linked_GlycosylationICICSQFSVPSSYHF
HHEECCCCCCCCCCC		26.02OGP
43O-linked_GlycosylationSQFSVPSSYHFTEDP
CCCCCCCCCCCCCCC		19.29OGP
47O-linked_GlycosylationVPSSYHFTEDPGAFP
CCCCCCCCCCCCCCC		26.60OGP
85N-linked_GlycosylationYDLFVHPNLTSLDFV
EEEECCCCCCCCCCH		40.8622106953
119N-linked_GlycosylationSKDLEITNATLQSEE
ECCCEECCCEECCHH		36.2716335952
135AcetylationSRYMKPGKELKVLSY
HCCCCCCCEEEEEEC		69.2920167786
138UbiquitinationMKPGKELKVLSYPAH
CCCCCEEEEEECCCH		42.07-
138AcetylationMKPGKELKVLSYPAH
CCCCCEEEEEECCCH		42.0720167786
155UbiquitinationIALLVPEKLTPHLKY
HHHHCCCCCCCCHHH		52.14-
157PhosphorylationLLVPEKLTPHLKYYV
HHCCCCCCCCHHHEE		21.5224719451
181UbiquitinationDGFEGFYKSTYRTLG
CCCCCEECCCEEECC		33.78-
219N-linked_GlycosylationDEPLFKANFSIKIRR
CCCCHHCCEEEEEEH		31.6122106953
238UbiquitinationIALSNMPKVKTIELE
EEECCCCCEEEEEEE		45.66-
260PhosphorylationFETTVKMSTYLVAYI
HHHHHHHHHHHHHHH		14.2625999147
280PhosphorylationSLSGFTSSGVKVSIY
HCCCCCCCCEEEEEE		44.5425999147
310PhosphorylationSLKLLDFYEKYFDIY
HHHHHHHHHHHHCEE		15.9224114839
405N-linked_GlycosylationYMELIAVNATYPELQ
HHHHHEEECCCCCCC		19.9722106953
437PhosphorylationLNSSRPISKPAETPT
CCCCCCCCCCCCCCH		34.9623401153
473UbiquitinationKDFLGEEKFQKGIIQ
HHHHCHHHHHHHHHH		49.12-
476UbiquitinationLGEEKFQKGIIQYLK
HCHHHHHHHHHHHHH		56.03-
484UbiquitinationGIIQYLKKFSYRNAK
HHHHHHHHHCCCCCC		36.63-
491UbiquitinationKFSYRNAKNDDLWSS
HHCCCCCCCCCHHHH		65.54-
506PhosphorylationLSNSCLESDFTSGGV
HCCHHCCCCCCCCCC		25.69-
516PhosphorylationTSGGVCHSDPKMTSN
CCCCCCCCCCCCCHH		50.94-
521O-linked_GlycosylationCHSDPKMTSNMLAFL
CCCCCCCCHHHHHHH		24.07OGP
521PhosphorylationCHSDPKMTSNMLAFL
CCCCCCCCHHHHHHH		24.0724043423
522PhosphorylationHSDPKMTSNMLAFLG
CCCCCCCHHHHHHHC		19.4224043423
539PhosphorylationAEVKEMMTTWTLQKG
HHHHHHHHHHHHCCC		20.1924043423
540PhosphorylationEVKEMMTTWTLQKGI
HHHHHHHHHHHCCCC		9.8824043423
542PhosphorylationKEMMTTWTLQKGIPL
HHHHHHHHHCCCCCE		19.7424043423
545UbiquitinationMTTWTLQKGIPLLVV
HHHHHHCCCCCEEEE		63.02-
553UbiquitinationGIPLLVVKQDGCSLR
CCCEEEECCCCCEEE		34.88-
606UbiquitinationVIHRHILKSKTDTLD
HHHHHHHHCCCCCCC		49.67-
607PhosphorylationIHRHILKSKTDTLDL
HHHHHHHCCCCCCCC		37.0222468782
608UbiquitinationHRHILKSKTDTLDLP
HHHHHHCCCCCCCCC		49.16-
609PhosphorylationRHILKSKTDTLDLPE
HHHHHCCCCCCCCCC		41.1122468782
611PhosphorylationILKSKTDTLDLPEKT
HHHCCCCCCCCCCCC		27.6622468782
617UbiquitinationDTLDLPEKTSWVKFN
CCCCCCCCCCEEEEE		46.01-
650N-linked_GlycosylationLITQLNQNHTLLRPK
HHHHHHHCCCCCCCH		29.1022106953
719PhosphorylationRRNISDISENLKRYL
CCCHHHHHHHHHHHH		25.98-
731UbiquitinationRYLLQYFKPVIDRQS
HHHHHHHHHHCCCCC		33.18-
831PhosphorylationILYALSTSKHQEKLL
HHHHHCCHHHHHHHH		25.4329457462
832UbiquitinationLYALSTSKHQEKLLK
HHHHCCHHHHHHHHH		49.77-
836UbiquitinationSTSKHQEKLLKLIEL
CCHHHHHHHHHHHHH		53.18-
899PhosphorylationYDIRMIISGTTAHFS
CEEEEEEECCCCCCC		21.11-
951PhosphorylationWLEKNLPTLRTWLMV
HHHHHCCHHHHHHCC		31.8523403867
954PhosphorylationKNLPTLRTWLMVNT-
HHCCHHHHHHCCCC-		26.5123403867
960PhosphorylationRTWLMVNT-------
HHHHCCCC-------		28.6923403867
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 ERAP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERAP2_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 ERAP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ERAP2_HUMAN !!
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 ERAP2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119, AND MASSSPECTROMETRY.

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