ERO1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ERO1B_HUMAN
• UniProt AC: Q86YB8
• Protein Name: ERO1-like protein beta
• Gene Name: ERO1B {ECO:0000312|HGNC:HGNC:14355}
• Organism: Homo sapiens (Human).
• Sequence Length: 467
• Subcellular Localization: Endoplasmic reticulum membrane ; Peripheral membrane protein ; Lumenal side . The association with ERP44 may be 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. Other protein disulfide isomerase family members can also be reoxidized, but at lower rates compared to P4HB, including PDIA2 (50% of P4HB reoxidation rate), as well as PDIA3, PDIA4, PDIA6 and NXNDC12 (<10%). Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. May be involved in oxidative proinsulin folding in pancreatic cells, hence may play a role in glucose homeostasis..
• Protein Sequence: MSQGVRRAGAGQGVAAAVQLLVTLSFLRSVVEAQVTGVLDDCLCDIDSIDNFNTYKIFPKIKKLQERDYFRYYKVNLKRPCPFWAEDGHCSIKDCHVEPCPESKIPVGIKAGHSNKYLKMANNTKELEDCEQANKLGAINSTLSNQSKEAFIDWARYDDSRDHFCELDDERSPAAQYVDLLLNPERYTGYKGTSAWRVWNSIYEENCFKPRSVYRPLNPLAPSRGEDDGESFYTWLEGLCLEKRVFYKLISGLHASINLHLCANYLLEETWGKPSWGPNIKEFKHRFDPVETKGEGPRRLKNLYFLYLIELRALSKVAPYFERSIVDLYTGNAEEDADTKTLLLNIFQDTKSFPMHFDEKSMFAGDKKGAKSLKEEFRLHFKNISRIMDCVGCDKCRLWGKLQTQGLGTALKILFSEKEIQKLPENSPSKGFQLTRQEIVALLNAFGRLSTSIRDLQNFKVLLQHSR

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
69	Phosphorylation	KKLQERDYFRYYKVN HHHHHHCCEEEEECC	9.00	-
72	Phosphorylation	QERDYFRYYKVNLKR HHHCCEEEEECCCCC	9.57	-
73	Phosphorylation	ERDYFRYYKVNLKRP HHCCEEEEECCCCCC	12.28	-
122	N-linked_Glycosylation	NKYLKMANNTKELED HHHHHHCCCCCCHHH	53.88	UniProtKB CARBOHYD
140	N-linked_Glycosylation	ANKLGAINSTLSNQS HHHHHHHHHHCCCCC	28.54	16263699
145	N-linked_Glycosylation	AINSTLSNQSKEAFI HHHHHCCCCCHHHHH	53.94	16263699
383	N-linked_Glycosylation	EFRLHFKNISRIMDC HHHHHHCCHHHHHHH	36.20	UniProtKB CARBOHYD
404	Phosphorylation	RLWGKLQTQGLGTAL HHHHHHHHCCHHHHH	34.73	-

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

Oops, there are no upstream regulatory protein records of ERO1B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ERO1B_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ERO1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ERP44_HUMAN	ERP44	physical	11847130
PDIA1_HUMAN	P4HB	physical	11847130
PDIA1_HUMAN	P4HB	physical	11707400
PDIA2_HUMAN	PDIA2	physical	20802462
PDIA3_HUMAN	PDIA3	physical	20802462
PDIA4_HUMAN	PDIA4	physical	20802462
ATP4A_HUMAN	ATP4A	physical	26186194
ERO1A_HUMAN	ERO1L	physical	26186194
FBX2_HUMAN	FBXO2	physical	26186194
GPX4_HUMAN	GPX4	physical	26344197
PSA4_HUMAN	PSMA4	physical	26344197
ATP4A_HUMAN	ATP4A	physical	28514442
ERO1A_HUMAN	ERO1L	physical	28514442
FBX2_HUMAN	FBXO2	physical	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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140, AND MASSSPECTROMETRY.
PubMed: 16263699