ERO1A_HUMAN - dbPTM
ERO1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERO1A_HUMAN
UniProt AC Q96HE7
Protein Name ERO1-like protein alpha
Gene Name ERO1A {ECO:0000312|HGNC:HGNC:13280}
Organism Homo sapiens (Human).
Sequence Length 468
Subcellular Localization Endoplasmic reticulum membrane
Peripheral membrane protein
Lumenal side . The association with ERP44 is essential for its retention in the endoplasmic reticulum.
Protein Description Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1..
Protein Sequence MGRGWGFLFGLLGAVWLLSSGHGEEQPPETAAQRCFCQVSGYLDDCTCDVETIDRFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDISQCGRRDCAVKPCQSDEVPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTIKRPLNPLASGQGTSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQETWLEKKWGHNITEFQQRFDGILTEGEGPRRLKNLYFLYLIELRALSKVLPFFERPDFQLFTGNKIQDEENKMLLLEILHEIKSFPLHFDENSFFAGDKKEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFHLTRQEIVSLFNAFGRISTSVKELENFRNLLQNIH
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
40PhosphorylationQRCFCQVSGYLDDCT
HHHHHHHHCCCCCCC		8.8830576142
47PhosphorylationSGYLDDCTCDVETID
HCCCCCCCCCCHHHH		20.8030576142
52PhosphorylationDCTCDVETIDRFNNY
CCCCCCHHHHCCCCC		28.2030576142
59PhosphorylationTIDRFNNYRLFPRLQ
HHHCCCCCCHHHHHH		15.14-
672-HydroxyisobutyrylationRLFPRLQKLLESDYF
CHHHHHHHHHHCCCH		60.68-
67UbiquitinationRLFPRLQKLLESDYF
CHHHHHHHHHHCCCH		60.6823000965
71PhosphorylationRLQKLLESDYFRYYK
HHHHHHHCCCHHEEE		37.2629449344
73PhosphorylationQKLLESDYFRYYKVN
HHHHHCCCHHEEECC		10.1519658100
75MethylationLLESDYFRYYKVNLK
HHHCCCHHEEECCCC		27.87-
102AcetylationGRRDCAVKPCQSDEV
CCCCCCCCCCCCCCC		22.8826822725
106PhosphorylationCAVKPCQSDEVPDGI
CCCCCCCCCCCCCCH		42.3226657352
115PhosphorylationEVPDGIKSASYKYSE
CCCCCHHHCHHHCCH		22.1125022875
120PhosphorylationIKSASYKYSEEANNL
HHHCHHHCCHHHHHH		17.0627486199
121PhosphorylationKSASYKYSEEANNLI
HHCHHHCCHHHHHHH		25.4727486199
131GlutathionylationANNLIEECEQAERLG
HHHHHHHHHHHHHHC		2.8122555962
143PhosphorylationRLGAVDESLSEETQK
HHCCCCHHCCHHHHH		32.5028355574
145PhosphorylationGAVDESLSEETQKAV
CCCCHHCCHHHHHHH		42.5425262027
150UbiquitinationSLSEETQKAVLQWTK
HCCHHHHHHHHHHHC		48.1321906983
166GlutathionylationDDSSDNFCEADDIQS
CCCCCCCCCCCCCCC		5.4522555962
192UbiquitinationPERYTGYKGPDAWKI
HHHHCCCCCCCHHHH		66.3729967540
208GlutathionylationNVIYEENCFKPQTIK
HHHHCCCCCCCCCCC		5.4022555962
210AcetylationIYEENCFKPQTIKRP
HHCCCCCCCCCCCCC		38.1126051181
248PhosphorylationCVEKRAFYRLISGLH
HHHHHHHHHHHHHHH		11.97-
266PhosphorylationNVHLSARYLLQETWL
HHHHHHHHHHHHHHH		16.10-
275AcetylationLQETWLEKKWGHNIT
HHHHHHHHHHCCCHH		52.2127452117
280N-linked_GlycosylationLEKKWGHNITEFQQR
HHHHHCCCHHHHHHH		38.6519159218
293PhosphorylationQRFDGILTEGEGPRR
HHHCCCCCCCCCHHH		39.77-
353PhosphorylationEILHEIKSFPLHFDE
HHHHHHHHCCCCCCC		37.44-
3682-HydroxyisobutyrylationNSFFAGDKKEAHKLK
CCCCCCCHHHHHHHH		52.15-
384N-linked_GlycosylationDFRLHFRNISRIMDC
HHHHHHCCHHHHHHH		35.33UniProtKB CARBOHYD
392UbiquitinationISRIMDCVGCFKCRL
HHHHHHHHHHHHHHH		6.9724816145
396UbiquitinationMDCVGCFKCRLWGKL
HHHHHHHHHHHHHHH		23.6324816145
3962-HydroxyisobutyrylationMDCVGCFKCRLWGKL
HHHHHHHHHHHHHHH		23.63-
405PhosphorylationRLWGKLQTQGLGTAL
HHHHHHHHCCHHHHH		34.73-
424SulfoxidationSEKLIANMPESGPSY
CHHHHHCCCCCCCCE		2.6230846556
431PhosphorylationMPESGPSYEFHLTRQ
CCCCCCCEEEEECHH		26.25-
451UbiquitinationFNAFGRISTSVKELE
HHHHHCCCCCHHHHH		17.1724816145
455UbiquitinationGRISTSVKELENFRN
HCCCCCHHHHHHHHH		57.2424816145
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
145SPhosphorylationKinaseFAM20CQ8IXL6
PSP
-KUbiquitinationE3 ubiquitin ligaseFBXO6Q9NRD1
PMID:27855403
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERO1A_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 ERO1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERP44_HUMANERP44physical
11847130
PDIA1_HUMANP4HBphysical
11847130
PDIA1_HUMANP4HBphysical
11707400
PDIA2_HUMANPDIA2physical
20802462
PDIA3_HUMANPDIA3physical
20802462
PDIA4_HUMANPDIA4physical
20802462
PELI2_HUMANPELI2physical
21988832
DDX5_HUMANDDX5physical
22863883
HPBP1_HUMANHSPBP1physical
22863883
LRSM1_HUMANLRSAM1physical
22863883
PPME1_HUMANPPME1physical
22863883
RINI_HUMANRNH1physical
22863883
WDR4_HUMANWDR4physical
22863883
GPX7_HUMANGPX7physical
21215271
GPX8_HUMANGPX8physical
21215271
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 ERO1A_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-280, AND MASSSPECTROMETRY.

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