2Y6E

Structure of the D1D2 domain of USP4, the conserved catalytic domain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004843	molecular_function	cysteine-type deubiquitinase activity
A	0016579	biological_process	protein deubiquitination
B	0004843	molecular_function	cysteine-type deubiquitinase activity
B	0016579	biological_process	protein deubiquitination
C	0004843	molecular_function	cysteine-type deubiquitinase activity
C	0016579	biological_process	protein deubiquitination
D	0004843	molecular_function	cysteine-type deubiquitinase activity
D	0016579	biological_process	protein deubiquitination
E	0004843	molecular_function	cysteine-type deubiquitinase activity
E	0016579	biological_process	protein deubiquitination
F	0004843	molecular_function	cysteine-type deubiquitinase activity
F	0016579	biological_process	protein deubiquitination

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1000

Chain	Residue
A	CYS461
A	CYS464
A	CYS799
A	CYS802

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 1926

Chain	Residue
B	ARG373
C	LYS348
C	ARG381
A	GLN391
A	MET877
A	GLY878
A	HOH2248
A	HOH2249

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1000

Chain	Residue
B	CYS461
B	CYS464
B	CYS799
B	CYS802

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 1000

Chain	Residue
C	CYS461
C	CYS464
C	CYS799
C	CYS802

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 1925

Chain	Residue
C	TYR476
C	THR478

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 1000

Chain	Residue
D	CYS461
D	CYS464
D	CYS799
D	CYS802

---

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN E 1000

Chain	Residue
E	CYS461
E	CYS464

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN F 1000

Chain	Residue
F	CYS461
F	CYS464

---

Functional Information from PROSITE/UniProt

site_id	PS00972
Number of Residues	16
Details	USP_1 Ubiquitin specific protease (USP) domain signature 1. GLgnlGNtCFMNSaLQ

Chain	Residue	Details
A	GLY303-GLN318

---

site_id	PS00973
Number of Residues	18
Details	USP_2 Ubiquitin specific protease (USP) domain signature 2. YdLiAVsnHyGamgv..GHY

Chain	Residue	Details
A	TYR865-TYR882

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Region: {"description":"Regulates ubiquitin dissociation","evidences":[{"source":"PubMed","id":"25404403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Region: {"description":"Necessary for interaction with RBL2","evidences":[{"source":"UniProtKB","id":"P35123","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	Region: {"description":"Necessary for interaction with RB1 and RBL2","evidences":[{"source":"UniProtKB","id":"P35123","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"11571652","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01035","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01035","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25404403","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y6E","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"30514904","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---