1FBV

STRUCTURE OF A CBL-UBCH7 COMPLEX: RING DOMAIN FUNCTION IN UBIQUITIN-PROTEIN LIGASES

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001784	molecular_function	phosphotyrosine residue binding
A	0004842	molecular_function	ubiquitin-protein transferase activity
A	0005509	molecular_function	calcium ion binding
A	0007166	biological_process	cell surface receptor signaling pathway
A	0023051	biological_process	regulation of signaling
A	0046872	molecular_function	metal ion binding
C	0000151	cellular_component	ubiquitin ligase complex
C	0000166	molecular_function	nucleotide binding
C	0000209	biological_process	protein polyubiquitination
C	0003713	molecular_function	transcription coactivator activity
C	0003723	molecular_function	RNA binding
C	0004842	molecular_function	ubiquitin-protein transferase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006355	biological_process	regulation of DNA-templated transcription
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
C	0008283	biological_process	cell population proliferation
C	0016567	biological_process	protein ubiquitination
C	0016740	molecular_function	transferase activity
C	0019787	molecular_function	ubiquitin-like protein transferase activity
C	0019899	molecular_function	enzyme binding
C	0031398	biological_process	positive regulation of protein ubiquitination
C	0031625	molecular_function	ubiquitin protein ligase binding
C	0032446	biological_process	protein modification by small protein conjugation
C	0036211	biological_process	protein modification process
C	0044770	biological_process	cell cycle phase transition
C	0045893	biological_process	positive regulation of DNA-templated transcription
C	0061631	molecular_function	ubiquitin conjugating enzyme activity
C	0070979	biological_process	protein K11-linked ubiquitination
C	0071383	biological_process	cellular response to steroid hormone stimulus
C	0071385	biological_process	cellular response to glucocorticoid stimulus
C	0097027	molecular_function	ubiquitin-protein transferase activator activity
C	1903955	biological_process	positive regulation of protein targeting to mitochondrion

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1001

Chain	Residue
A	CYS381
A	CYS384
A	CYS401
A	CYS404

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1002

Chain	Residue
A	CYS396
A	HIS398
A	CYS416
A	CYS419

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 2001

Chain	Residue
A	ARG68
A	LYS65

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 2002

Chain	Residue
A	HIS213
A	SER253
A	LEU254
A	LEU255
A	ARG256
A	HIS360

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 2003

Chain	Residue
A	ARG180
A	LYS183
A	ARG246
A	GLN249

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 2004

Chain	Residue
A	GLN146
A	ARG149
A	LYS153
A	MET374

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 2005

Chain	Residue
A	LYS382
C	LYS1009
C	LYS1100

---

Functional Information from PROSITE/UniProt

site_id	PS00183
Number of Residues	16
Details	UBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNIdek.GqVCLpvI

Chain	Residue	Details
C	TYR1075-ILE1090

---

site_id	PS00518
Number of Residues	10
Details	ZF_RING_1 Zinc finger RING-type signature. CgHlMCtsCL

Chain	Residue	Details
A	CYS396-LEU405

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	304
Details	Domain: {"description":"Cbl-PTB","evidences":[{"source":"PROSITE-ProRule","id":"PRU00839","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	39
Details	Zinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	128
Details	Region: {"description":"4H"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	72
Details	Region: {"description":"EF-hand-like"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	102
Details	Region: {"description":"SH2-like"}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	28
Details	Region: {"description":"Linker"}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PDB","id":"1B47","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CBL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by INSR","evidences":[{"source":"PubMed","id":"11997497","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	1
Details	M-CSA 438

Chain	Residue	Details
C	CYS1086	nucleofuge

---