3A1Q

Crystal structure of the mouse RAP80 UIMs in complex with Lys63-linked di-ubiquitin

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0006302	biological_process	double-strand break repair
C	0070530	molecular_function	K63-linked polyubiquitin modification-dependent protein binding
C	0070531	cellular_component	BRCA1-A complex
F	0006302	biological_process	double-strand break repair
F	0070530	molecular_function	K63-linked polyubiquitin modification-dependent protein binding
F	0070531	cellular_component	BRCA1-A complex

Functional Information from PROSITE/UniProt

site_id	PS00299
Number of Residues	26
Details	UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD

Chain	Residue	Details
B	LYS27-ASP52
A	LYS27-ASP52

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:Q96RL1

Chain	Residue	Details
C	LYS90
B	ARG72
F	LYS90
E	ARG72

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Essential for function

Chain	Residue	Details
B	HIS68
E	HIS68

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P0CG48

Chain	Residue	Details
B	SER65
E	SER65

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: ADP-ribosylglycine => ECO:0000250|UniProtKB:P0CG48

Chain	Residue	Details
B	GLY76
E	GLY76

---

site_id	SWS_FT_FI5
Number of Residues	14
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48

Chain	Residue	Details
B	LYS6
E	LYS27
E	LYS29
E	LYS33
E	LYS48
E	ARG63
B	LYS11
B	LYS27
B	LYS29
B	LYS33
B	LYS48
B	ARG63
E	LYS6
E	LYS11

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214

Chain	Residue	Details
B	GLY76
E	GLY76

---