EPO_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EPO_HUMAN
• UniProt AC: P01588
• Protein Name: Erythropoietin
• Gene Name: EPO
• Organism: Homo sapiens (Human).
• Sequence Length: 193
• Subcellular Localization: Secreted.
• Protein Description: Hormone involved in the regulation of erythrocyte proliferation and differentiation and the maintenance of a physiological level of circulating erythrocyte mass. Binds to EPOR leading to EPOR dimerization and JAK2 activation thereby activating specific downstream effectors, including STAT1 and STAT3..
• Protein Sequence: MGVHECPAWLWLLLSLLSLPLGLPVLGAPPRLICDSRVLERYLLEAKEAENITTGCAEHCSLNENITVPDTKVNFYAWKRMEVGQQAVEVWQGLALLSEAVLRGQALLVNSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRTGDR

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
51	N-linked_Glycosylation	LEAKEAENITTGCAE HHHHHHHCCCCHHHH	43.91	3949763
51	N-linked_Glycosylation	LEAKEAENITTGCAE HHHHHHHCCCCHHHH	43.91	3949763
54	Sulfoxidation	KEAENITTGCAEHCS HHHHCCCCHHHHHCC	26.85	18661870
65	N-linked_Glycosylation	EHCSLNENITVPDTK HHCCCCCCCCCCCCC	33.87	3949763
65	N-linked_Glycosylation	EHCSLNENITVPDTK HHCCCCCCCCCCCCC	33.87	3949763
110	N-linked_Glycosylation	RGQALLVNSSQPWEP HCCEEECCCCCCCCC	35.59	3949763
110	N-linked_Glycosylation	RGQALLVNSSQPWEP HCCEEECCCCCCCCC	35.59	3949763
111	Phosphorylation	GQALLVNSSQPWEPL CCEEECCCCCCCCCE	23.91	18452278
127	Phosphorylation	LHVDKAVSGLRSLTT HHHHHHHHHHHHHHH	36.65	18452278
131	Phosphorylation	KAVSGLRSLTTLLRA HHHHHHHHHHHHHHH	34.80	-
133	Phosphorylation	VSGLRSLTTLLRALG HHHHHHHHHHHHHHC	19.35	21964256
134	Phosphorylation	SGLRSLTTLLRALGA HHHHHHHHHHHHHCC	29.14	21964256
153	O-linked_Glycosylation	ISPPDAASAAPLRTI CCCCCHHHCCCCCEE	27.04	3949763
153	O-linked_Glycosylation	ISPPDAASAAPLRTI CCCCCHHHCCCCCEE	27.04	3949763
161	Phosphorylation	AAPLRTITADTFRKL CCCCCEECHHHHHHH	20.19	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EPO_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 EPO_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EPOR_HUMAN	EPOR	physical	10318834
EPOR_HUMAN	EPOR	physical	9808045
EPOR_HUMAN	EPOR	physical	17327410
EPOR_HUMAN	EPOR	physical	15358619
EPOR_HUMAN	EPOR	physical	28514442
GINM1_HUMAN	GINM1	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 612623: Microvascular complications of diabetes 2 (MVCD2)
• 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

"Structural characterization of human erythropoietin.";
Lai P.H., Everett R., Wang F.F., Arakawa T., Goldwasser E.;
J. Biol. Chem. 261:3116-3121(1986).
Cited for: PROTEIN SEQUENCE OF 28-193, AND DISULFIDE BONDS.
PubMed: 3949763

O-linked Glycosylation

"Structural characterization of human erythropoietin.";
Lai P.H., Everett R., Wang F.F., Arakawa T., Goldwasser E.;
J. Biol. Chem. 261:3116-3121(1986).
Cited for: PROTEIN SEQUENCE OF 28-193, AND DISULFIDE BONDS.
PubMed: 3949763