10FT

Cryo-EM structure of receptor tyrosine kinase ROS1 in complex with NELL2

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0005080	molecular_function	protein kinase C binding
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0008201	molecular_function	heparin binding
B	0009566	biological_process	fertilization
B	0042802	molecular_function	identical protein binding
B	0070050	biological_process	neuron cellular homeostasis
B	0071679	biological_process	commissural neuron axon guidance
B	0140149	cellular_component	non-collagenous component of interstitial matrix

Functional Information from PROSITE/UniProt

site_id	PS00010
Number of Residues	12
Details	ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CvNtpgsFmCiC

Chain	Residue	Details
B	CYS457-CYS468
B	CYS572-CYS583
B	CYS619-CYS630

---

site_id	PS00022
Number of Residues	12
Details	EGF_1 EGF-like domain signature 1. CaCpqGftGPsC

Chain	Residue	Details
B	CYS541-CYS552

---

site_id	PS01186
Number of Residues	15
Details	EGF_2 EGF-like domain signature 2. CiCktGYiriddys.C

Chain	Residue	Details
B	CYS466-CYS480
B	CYS508-CYS521
B	CYS541-CYS552
B	CYS663-CYS677

---

site_id	PS01187
Number of Residues	27
Details	EGF_CA Calcium-binding EGF-like domain signature. DiDECaegrhy........Crentm..CvNtpgsFmC

Chain	Residue	Details
B	ASP440-CYS466
B	ASP555-CYS581
B	ASP602-CYS628

---

site_id	PS01208
Number of Residues	40
Details	VWFC_1 VWFC domain signature. Ckn.CTClngtiq........CetliCpnpd......Cplksalayvdgk....CCke..C

Chain	Residue	Details
B	CYS291-CYS330
B	CYS719-CYS755

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	59
Details	Domain: {"description":"VWFC 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00220","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	42
Details	Domain: {"description":"EGF-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	41
Details	Domain: {"description":"EGF-like 2; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32198364","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6POG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	95
Details	Domain: {"description":"Fibronectin type-III 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	88
Details	Domain: {"description":"Fibronectin type-III 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	100
Details	Domain: {"description":"Fibronectin type-III 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---