1EER

CRYSTAL STRUCTURE OF HUMAN ERYTHROPOIETIN COMPLEXED TO ITS RECEPTOR AT 1.9 ANGSTROMS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0001666	biological_process	response to hypoxia
A	0005125	molecular_function	cytokine activity
A	0005128	molecular_function	erythropoietin receptor binding
A	0005179	molecular_function	hormone activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0006915	biological_process	apoptotic process
A	0006950	biological_process	response to stress
A	0006953	biological_process	acute-phase response
A	0007165	biological_process	signal transduction
A	0007566	biological_process	embryo implantation
A	0007584	biological_process	response to nutrient
A	0008015	biological_process	blood circulation
A	0008284	biological_process	positive regulation of cell population proliferation
A	0009651	biological_process	response to salt stress
A	0009986	cellular_component	cell surface
A	0010523	biological_process	negative regulation of calcium ion transport into cytosol
A	0010976	biological_process	positive regulation of neuron projection development
A	0030218	biological_process	erythrocyte differentiation
A	0030295	molecular_function	protein kinase activator activity
A	0032496	biological_process	response to lipopolysaccharide
A	0033028	biological_process	myeloid cell apoptotic process
A	0033033	biological_process	negative regulation of myeloid cell apoptotic process
A	0033189	biological_process	response to vitamin A
A	0033574	biological_process	response to testosterone
A	0038162	biological_process	erythropoietin-mediated signaling pathway
A	0042104	biological_process	positive regulation of activated T cell proliferation
A	0042541	biological_process	hemoglobin biosynthetic process
A	0043066	biological_process	negative regulation of apoptotic process
A	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
A	0043249	biological_process	erythrocyte maturation
A	0043627	biological_process	response to estrogen
A	0044297	cellular_component	cell body
A	0045666	biological_process	positive regulation of neuron differentiation
A	0045893	biological_process	positive regulation of DNA-templated transcription
A	0046579	biological_process	positive regulation of Ras protein signal transduction
A	0048678	biological_process	response to axon injury
A	0051602	biological_process	response to electrical stimulus
A	0055093	biological_process	response to hyperoxia
A	0070374	biological_process	positive regulation of ERK1 and ERK2 cascade
A	0070555	biological_process	response to interleukin-1
A	0071474	biological_process	cellular hyperosmotic response
A	0071548	biological_process	response to dexamethasone
A	0097696	biological_process	cell surface receptor signaling pathway via STAT
A	1902219	biological_process	negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress
A	1902251	biological_process	negative regulation of erythrocyte apoptotic process
B	0004896	molecular_function	cytokine receptor activity
B	0016020	cellular_component	membrane
C	0004896	molecular_function	cytokine receptor activity
C	0016020	cellular_component	membrane

Functional Information from PROSITE/UniProt

site_id	PS00817
Number of Residues	28
Details	EPO_TPO Erythropoietin / thrombopoeitin signature. PprliCDsRVLeRylleakeaekittgC

Chain	Residue	Details
A	PRO2-CYS29

---

site_id	PS01352
Number of Residues	81
Details	HEMATOPO_REC_L_F1 Long hematopoietin receptor, single chain family signature. VvLrWlpppetpmtshir...YEVdvsagqgagsvqrveilegrtecvlsnLrgrtrytfavRaRmaepsfggfWseWsepvsL

Chain	Residue	Details
B	VAL138-LEU218

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000052","evidences":[{"source":"PubMed","id":"3949763","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000166","evidences":[{"source":"PubMed","id":"3949763","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000192","evidences":[{"source":"PubMed","id":"3949763","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"O-linked (GalNAc...) serine","evidences":[{"source":"PubMed","id":"3949763","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Motif: {"description":"WSXWS motif","evidences":[{"source":"PubMed","id":"9774108","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Site: {"description":"Required for ligand binding","evidences":[{"source":"PubMed","id":"8662939","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---