4WSN | pdb_00004wsn

Crystal structure of the COP9 signalosome, a P1 crystal form

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
V	SCOP2B Superfamily	JAB1/MPN domain-like	8053244	3001105	SCOP2B (2022-06-29)
V	SCOP2B Superfamily	EIF3 subunit F C-terminal domain-like	8053243	3002167	SCOP2B (2022-06-29)
TA [auth t]	SCOP2B Superfamily	JAB1/MPN domain-like	8053244	3001105	SCOP2B (2022-06-29)
TA [auth t]	SCOP2B Superfamily	EIF3 subunit F C-terminal domain-like	8053243	3002167	SCOP2B (2022-06-29)
N	SCOP2B Superfamily	JAB1/MPN domain-like	8053244	3001105	SCOP2B (2022-06-29)
N	SCOP2B Superfamily	EIF3 subunit F C-terminal domain-like	8053243	3002167	SCOP2B (2022-06-29)
LA [auth l]	SCOP2B Superfamily	EIF3 subunit F C-terminal domain-like	8053243	3002167	SCOP2B (2022-06-29)
LA [auth l]	SCOP2B Superfamily	JAB1/MPN domain-like	8053244	3001105	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	JAB1/MPN domain-like	8053244	3001105	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	EIF3 subunit F C-terminal domain-like	8053243	3002167	SCOP2B (2022-06-29)
DA [auth d]	SCOP2B Superfamily	EIF3 subunit F C-terminal domain-like	8053243	3002167	SCOP2B (2022-06-29)
DA [auth d]	SCOP2B Superfamily	JAB1/MPN domain-like	8053244	3001105	SCOP2B (2022-06-29)
U	SCOP2B Superfamily	JAB1/MPN domain-like	8053263	3001105	SCOP2B (2022-06-29)
SA [auth s]	SCOP2B Superfamily	JAB1/MPN domain-like	8053263	3001105	SCOP2B (2022-06-29)
M	SCOP2B Superfamily	JAB1/MPN domain-like	8053263	3001105	SCOP2B (2022-06-29)
KA [auth k]	SCOP2B Superfamily	JAB1/MPN domain-like	8053263	3001105	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	JAB1/MPN domain-like	8053263	3001105	SCOP2B (2022-06-29)
CA [auth c]	SCOP2B Superfamily	JAB1/MPN domain-like	8053263	3001105	SCOP2B (2022-06-29)
Y	SCOP2B Superfamily	TPR-like	8057037	3001345	SCOP2B (2022-06-29)
Y	SCOP2B Superfamily	TPR-like	8057036	3001345	SCOP2B (2022-06-29)
Y	SCOP2B Superfamily	Winged helix DNA-binding domain	8057039	3000034	SCOP2B (2022-06-29)
Q	SCOP2B Superfamily	TPR-like	8057037	3001345	SCOP2B (2022-06-29)
Q	SCOP2B Superfamily	TPR-like	8057036	3001345	SCOP2B (2022-06-29)
Q	SCOP2B Superfamily	Winged helix DNA-binding domain	8057039	3000034	SCOP2B (2022-06-29)
OA [auth o]	SCOP2B Superfamily	TPR-like	8057037	3001345	SCOP2B (2022-06-29)
OA [auth o]	SCOP2B Superfamily	Winged helix DNA-binding domain	8057039	3000034	SCOP2B (2022-06-29)
OA [auth o]	SCOP2B Superfamily	TPR-like	8057036	3001345	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Winged helix DNA-binding domain	8057039	3000034	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	TPR-like	8057036	3001345	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	TPR-like	8057037	3001345	SCOP2B (2022-06-29)
GA [auth g]	SCOP2B Superfamily	TPR-like	8057036	3001345	SCOP2B (2022-06-29)
GA [auth g]	SCOP2B Superfamily	TPR-like	8057037	3001345	SCOP2B (2022-06-29)
GA [auth g]	SCOP2B Superfamily	Winged helix DNA-binding domain	8057039	3000034	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Winged helix DNA-binding domain	8057039	3000034	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	TPR-like	8057037	3001345	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	TPR-like	8057036	3001345	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
X	CSN8_PSD8_EIF3K_C_1	e4wsnX2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: CSN8_PSD8_EIF3K_C_1	ECOD (1.6)
X	CSN8_PSD8_EIF3K_N	e4wsnX1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: CSN8_PSD8_EIF3K_N	ECOD (1.6)
VA [auth v]	CSN8_PSD8_EIF3K_C_1	e4wsnv1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: CSN8_PSD8_EIF3K_C_1	ECOD (1.6)
VA [auth v]	CSN8_PSD8_EIF3K_N	e4wsnv2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: CSN8_PSD8_EIF3K_N	ECOD (1.6)
P	CSN8_PSD8_EIF3K_C_1	e4wsnP1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: CSN8_PSD8_EIF3K_C_1	ECOD (1.6)
P	CSN8_PSD8_EIF3K_N	e4wsnP2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: CSN8_PSD8_EIF3K_N	ECOD (1.6)
NA [auth n]	CSN8_PSD8_EIF3K_C_1	e4wsnn1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: CSN8_PSD8_EIF3K_C_1	ECOD (1.6)
NA [auth n]	CSN8_PSD8_EIF3K_N	e4wsnn2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: CSN8_PSD8_EIF3K_N	ECOD (1.6)
H	CSN8_PSD8_EIF3K_C_1	e4wsnH2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: CSN8_PSD8_EIF3K_C_1	ECOD (1.6)
H	CSN8_PSD8_EIF3K_N	e4wsnH1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: CSN8_PSD8_EIF3K_N	ECOD (1.6)
FA [auth f]	CSN8_PSD8_EIF3K_C_1	e4wsnf1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: CSN8_PSD8_EIF3K_C_1	ECOD (1.6)
FA [auth f]	CSN8_PSD8_EIF3K_N	e4wsnf2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: CSN8_PSD8_EIF3K_N	ECOD (1.6)
W	PCI	e4wsnW1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI	ECOD (1.6)
W	KOG3250_1st	e4wsnW2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG3250_1st	ECOD (1.6)
W	KOG3250_2nd	e4wsnW3	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN9 C-terminal helix	F: KOG3250_2nd	ECOD (1.6)
UA [auth u]	PCI	e4wsnu3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI	ECOD (1.6)
UA [auth u]	KOG3250_1st	e4wsnu2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG3250_1st	ECOD (1.6)
UA [auth u]	KOG3250_2nd	e4wsnu1	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN9 C-terminal helix	F: KOG3250_2nd	ECOD (1.6)
O	PCI	e4wsnO3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI	ECOD (1.6)
O	KOG3250_1st	e4wsnO1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG3250_1st	ECOD (1.6)
O	KOG3250_2nd	e4wsnO2	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN9 C-terminal helix	F: KOG3250_2nd	ECOD (1.6)
MA [auth m]	PCI	e4wsnm3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI	ECOD (1.6)
MA [auth m]	KOG3250_1st	e4wsnm1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG3250_1st	ECOD (1.6)
MA [auth m]	KOG3250_2nd	e4wsnm2	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN9 C-terminal helix	F: KOG3250_2nd	ECOD (1.6)
G	PCI	e4wsnG2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI	ECOD (1.6)
G	KOG3250_1st	e4wsnG1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG3250_1st	ECOD (1.6)
G	KOG3250_2nd	e4wsnG3	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN9 C-terminal helix	F: KOG3250_2nd	ECOD (1.6)
EA [auth e]	PCI	e4wsne2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI	ECOD (1.6)
EA [auth e]	KOG3250_1st	e4wsne3	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG3250_1st	ECOD (1.6)
EA [auth e]	KOG3250_2nd	e4wsne1	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN9 C-terminal helix	F: KOG3250_2nd	ECOD (1.6)
V	JAB_1	e4wsnV1	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: JAB_1	ECOD (1.6)
V	MitMem_reg	e4wsnV2	A: extended segments	X: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain	F: MitMem_reg	ECOD (1.6)
TA [auth t]	JAB_1	e4wsnt1	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: JAB_1	ECOD (1.6)
TA [auth t]	MitMem_reg	e4wsnt2	A: extended segments	X: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain	F: MitMem_reg	ECOD (1.6)
N	JAB_1	e4wsnN2	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: JAB_1	ECOD (1.6)
N	MitMem_reg	e4wsnN3	A: extended segments	X: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain	F: MitMem_reg	ECOD (1.6)
LA [auth l]	JAB_1	e4wsnl2	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: JAB_1	ECOD (1.6)
LA [auth l]	MitMem_reg	e4wsnl3	A: extended segments	X: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain	F: MitMem_reg	ECOD (1.6)
F	JAB_1	e4wsnF2	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: JAB_1	ECOD (1.6)
F	MitMem_reg	e4wsnF3	A: extended segments	X: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain	F: MitMem_reg	ECOD (1.6)
DA [auth d]	JAB_1	e4wsnd1	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: JAB_1	ECOD (1.6)
DA [auth d]	MitMem_reg	e4wsnd2	A: extended segments	X: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain	F: MitMem_reg	ECOD (1.6)
U	JAB	e4wsnU1	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: JAB	ECOD (1.6)
U	KOG1554	e4wsnU2	A: extended segments	X: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain	F: KOG1554	ECOD (1.6)
SA [auth s]	JAB	e4wsns2	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: JAB	ECOD (1.6)
SA [auth s]	KOG1554	e4wsns1	A: extended segments	X: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain	F: KOG1554	ECOD (1.6)
M	JAB	e4wsnM1	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: JAB	ECOD (1.6)
M	KOG1554	e4wsnM2	A: extended segments	X: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain	F: KOG1554	ECOD (1.6)
KA [auth k]	JAB	e4wsnk1	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: JAB	ECOD (1.6)
KA [auth k]	KOG1554	e4wsnk2	A: extended segments	X: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain	F: KOG1554	ECOD (1.6)
E	JAB	e4wsnE2	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: JAB	ECOD (1.6)
E	KOG1554	e4wsnE1	A: extended segments	X: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain	F: KOG1554	ECOD (1.6)
CA [auth c]	JAB	e4wsnc2	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: JAB	ECOD (1.6)
CA [auth c]	KOG1554	e4wsnc1	A: extended segments	X: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)	T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain	F: KOG1554	ECOD (1.6)
T	PCI	e4wsnT3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI	ECOD (1.6)
T	RPN7_1	e4wsnT1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: RPN7_1	ECOD (1.6)
T	KOG1497	e4wsnT2	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN5 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN5 C-terminal helix	F: KOG1497	ECOD (1.6)
RA [auth r]	PCI	e4wsnr2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI	ECOD (1.6)
RA [auth r]	RPN7_1	e4wsnr1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: RPN7_1	ECOD (1.6)
RA [auth r]	KOG1497	e4wsnr3	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN5 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN5 C-terminal helix	F: KOG1497	ECOD (1.6)
L	PCI	e4wsnL2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI	ECOD (1.6)
L	RPN7_1	e4wsnL1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: RPN7_1	ECOD (1.6)
L	KOG1497	e4wsnL3	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN5 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN5 C-terminal helix	F: KOG1497	ECOD (1.6)
JA [auth j]	PCI	e4wsnj1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI	ECOD (1.6)
JA [auth j]	RPN7_1	e4wsnj2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: RPN7_1	ECOD (1.6)
JA [auth j]	KOG1497	e4wsnj3	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN5 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN5 C-terminal helix	F: KOG1497	ECOD (1.6)
D	PCI	e4wsnD2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI	ECOD (1.6)
D	RPN7_1	e4wsnD1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: RPN7_1	ECOD (1.6)
D	KOG1497	e4wsnD3	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN5 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN5 C-terminal helix	F: KOG1497	ECOD (1.6)
BA [auth b]	PCI	e4wsnb3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI	ECOD (1.6)
BA [auth b]	RPN7_1	e4wsnb2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: RPN7_1	ECOD (1.6)
BA [auth b]	KOG1497	e4wsnb1	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN5 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN5 C-terminal helix	F: KOG1497	ECOD (1.6)
S	PCI,KOG2581	e4wsnS3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI,KOG2581	ECOD (1.6)
S	KOG2581	e4wsnS2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG2581	ECOD (1.6)
S	KOG2582_like	e4wsnS1	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN3 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN3 C-terminal helix	F: KOG2582_like	ECOD (1.6)
QA [auth q]	PCI,KOG2581	e4wsnq3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI,KOG2581	ECOD (1.6)
QA [auth q]	KOG2581	e4wsnq2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG2581	ECOD (1.6)
QA [auth q]	KOG2582_like	e4wsnq1	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN3 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN3 C-terminal helix	F: KOG2582_like	ECOD (1.6)
K	PCI,KOG2581	e4wsnK2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI,KOG2581	ECOD (1.6)
K	KOG2581	e4wsnK1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG2581	ECOD (1.6)
K	KOG2582_like	e4wsnK3	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN3 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN3 C-terminal helix	F: KOG2582_like	ECOD (1.6)
IA [auth i]	PCI,KOG2581	e4wsni3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI,KOG2581	ECOD (1.6)
IA [auth i]	KOG2581	e4wsni1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG2581	ECOD (1.6)
IA [auth i]	KOG2582_like	e4wsni2	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN3 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN3 C-terminal helix	F: KOG2582_like	ECOD (1.6)
C	PCI,KOG2581	e4wsnC1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI,KOG2581	ECOD (1.6)
C	KOG2581	e4wsnC3	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG2581	ECOD (1.6)
C	KOG2582_like	e4wsnC2	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN3 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN3 C-terminal helix	F: KOG2582_like	ECOD (1.6)
AA [auth a]	PCI,KOG2581	e4wsna3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI,KOG2581	ECOD (1.6)
AA [auth a]	KOG2581	e4wsna2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG2581	ECOD (1.6)
AA [auth a]	KOG2582_like	e4wsna1	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN3 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN3 C-terminal helix	F: KOG2582_like	ECOD (1.6)
Z	PCI_1	e4wsnZ1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI_1	ECOD (1.6)
Z	KOG2581	e4wsnZ2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG2581	ECOD (1.6)
Z	KOG1464	e4wsnZ3	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN9 C-terminal helix	F: KOG1464	ECOD (1.6)
R	PCI_1	e4wsnR2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI_1	ECOD (1.6)
R	KOG2581	e4wsnR1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG2581	ECOD (1.6)
R	KOG1464	e4wsnR3	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN9 C-terminal helix	F: KOG1464	ECOD (1.6)
PA [auth p]	PCI_1	e4wsnp1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI_1	ECOD (1.6)
PA [auth p]	KOG2581	e4wsnp2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG2581	ECOD (1.6)
PA [auth p]	KOG1464	e4wsnp3	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN9 C-terminal helix	F: KOG1464	ECOD (1.6)
J	PCI_1	e4wsnJ3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI_1	ECOD (1.6)
J	KOG2581	e4wsnJ2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG2581	ECOD (1.6)
J	KOG1464	e4wsnJ1	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN9 C-terminal helix	F: KOG1464	ECOD (1.6)
HA [auth h]	PCI_1	e4wsnh2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI_1	ECOD (1.6)
HA [auth h]	KOG2581	e4wsnh3	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG2581	ECOD (1.6)
HA [auth h]	KOG1464	e4wsnh1	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN9 C-terminal helix	F: KOG1464	ECOD (1.6)
B	PCI_1	e4wsnB2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI_1	ECOD (1.6)
B	KOG2581	e4wsnB1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: KOG2581	ECOD (1.6)
B	KOG1464	e4wsnB3	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN9 C-terminal helix	F: KOG1464	ECOD (1.6)
Y	PCI_2	e4wsnY3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI_2	ECOD (1.6)
Y	RPN7	e4wsnY2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: RPN7	ECOD (1.6)
Y	KOG0686_2nd	e4wsnY1	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN7 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN7 C-terminal helix	F: KOG0686_2nd	ECOD (1.6)
Q	PCI_2	e4wsnQ3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI_2	ECOD (1.6)
Q	RPN7	e4wsnQ2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: RPN7	ECOD (1.6)
Q	KOG0686_2nd	e4wsnQ1	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN7 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN7 C-terminal helix	F: KOG0686_2nd	ECOD (1.6)
OA [auth o]	PCI_2	e4wsno4	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI_2	ECOD (1.6)
OA [auth o]	RPN7	e4wsno3	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: RPN7	ECOD (1.6)
OA [auth o]	KOG0686_2nd	e4wsno2	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN7 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN7 C-terminal helix	F: KOG0686_2nd	ECOD (1.6)
I	PCI_2	e4wsnI3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI_2	ECOD (1.6)
I	RPN7	e4wsnI1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: RPN7	ECOD (1.6)
I	KOG0686_2nd	e4wsnI2	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN7 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN7 C-terminal helix	F: KOG0686_2nd	ECOD (1.6)
GA [auth g]	PCI_2	e4wsng2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI_2	ECOD (1.6)
GA [auth g]	RPN7	e4wsng1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: RPN7	ECOD (1.6)
GA [auth g]	KOG0686_2nd	e4wsng3	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN7 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN7 C-terminal helix	F: KOG0686_2nd	ECOD (1.6)
A	PCI_2	e4wsnA2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: PCI_2	ECOD (1.6)
A	RPN7	e4wsnA1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: RPN7	ECOD (1.6)
A	KOG0686_2nd	e4wsnA3	A: extended segments	X: 26S proteasome regulatory subunits C-terminal helices	H: 26S proteasome regulatory subunit RPN7 C-terminal helix (From Topology)	T: 26S proteasome regulatory subunit RPN7 C-terminal helix	F: KOG0686_2nd	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
FA [auth f], H, NA [auth n], P, VA [auth v], FA [auth f], H, NA [auth n], P, VA [auth v], X	PF10075	CSN8/PSMD8/EIF3K family (CSN8_PSD8_EIF3K)	CSN8/PSMD8/EIF3K family	-	Family
EA [auth e], G, MA [auth m], O, UA [auth u], EA [auth e], G, MA [auth m], O, UA [auth u], W	PF22061	CSN7 helical bundle subdomain (CSN7_HB_subdom)	CSN7 helical bundle subdomain	-	Repeat
EA [auth e], G, MA [auth m], O, UA [auth u], EA [auth e], G, MA [auth m], O, UA [auth u], W	PF18392	COP9 signalosome complex subunit 7a helix I domain (CSN7a_helixI)	COP9 signalosome complex subunit 7a helix I domain	This is The C-terminal helix I domain found in COP9 signalosome complex subunit 7a. The helix from CSN7 (helix I) contacts CSN6 helices I and II at the base of the bundle, nearest the PCI ring [1].	Domain
EA [auth e], G, MA [auth m], O, UA [auth u], EA [auth e], G, MA [auth m], O, UA [auth u], W	PF10602	26S proteasome subunit RPN7 (RPN7)	26S proteasome subunit RPN7	-	Repeat
EA [auth e], G, MA [auth m], O, UA [auth u], EA [auth e], G, MA [auth m], O, UA [auth u], W	PF01399	PCI domain (PCI)	PCI domain	This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].	Domain
DA [auth d], F, LA [auth l], N, TA [auth t], DA [auth d], F, LA [auth l], N, TA [auth t], V	PF10075	CSN8/PSMD8/EIF3K family (CSN8_PSD8_EIF3K)	CSN8/PSMD8/EIF3K family	-	Family
DA [auth d], F, LA [auth l], N, TA [auth t], DA [auth d], F, LA [auth l], N, TA [auth t], V	PF13012	Maintenance of mitochondrial structure and function (MitMem_reg)	Maintenance of mitochondrial structure and function	-	Family
DA [auth d], F, LA [auth l], N, TA [auth t], DA [auth d], F, LA [auth l], N, TA [auth t], V	PF01398	JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)	JAB1/Mov34/MPN/PAD-1 ubiquitin protease	Proteins with this domain are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This domain is known as the MPN domain [3] and PAD-1-like domain [4], JABP1 domain [5] or J ...	Proteins with this domain are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This domain is known as the MPN domain [3] and PAD-1-like domain [4], JABP1 domain [5] or JAMM domain [7]. These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signalling and protein turnover pathways in eukaryotes [7]. Versions of the domain in prokaryotic cognates of the ubiquitin-modification pathway are shown to have a similar role, and the archaeal protein from Haloferax volcanii is found to cleave ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates [8,9].	Domain
CA [auth c], E, KA [auth k], M, SA [auth s], CA [auth c], E, KA [auth k], M, SA [auth s], U	PF18323	Cop9 signalosome subunit 5 C-terminal domain (CSN5_C)	Cop9 signalosome subunit 5 C-terminal domain	The COP9 (Constitutive photomorphogenesis 9) signalosome (CSN), a large multiprotein complex that resembles the 19S lid of the 26S proteasome, plays a central role in the regulation of the E3-cullin RING ubiquitin ligases (CRLs) [1]. The catalytic ac ...	The COP9 (Constitutive photomorphogenesis 9) signalosome (CSN), a large multiprotein complex that resembles the 19S lid of the 26S proteasome, plays a central role in the regulation of the E3-cullin RING ubiquitin ligases (CRLs) [1]. The catalytic activity of the CSN complex is carried by subunit 5 (CSN5), also known as c-Jun activation domain-binding protein-1 (Jab1) [1]. This entry is the C-terminal domain found in CSN5 proteins. CSN5, whose two C-terminal helices form an antiparallel hairpin, inserts its final C-terminal helix (helix II) into the central CSN6 framework at the core of the bundle. Deletion of the C-terminal helices has a pronounced effect on CSN integrity [2].	Domain
CA [auth c], E, KA [auth k], M, SA [auth s], CA [auth c], E, KA [auth k], M, SA [auth s], U	PF22061	CSN7 helical bundle subdomain (CSN7_HB_subdom)	CSN7 helical bundle subdomain	-	Repeat
CA [auth c], E, KA [auth k], M, SA [auth s], CA [auth c], E, KA [auth k], M, SA [auth s], U	PF01398	JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)	JAB1/Mov34/MPN/PAD-1 ubiquitin protease	Proteins with this domain are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This domain is known as the MPN domain [3] and PAD-1-like domain [4], JABP1 domain [5] or J ...	Proteins with this domain are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This domain is known as the MPN domain [3] and PAD-1-like domain [4], JABP1 domain [5] or JAMM domain [7]. These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signalling and protein turnover pathways in eukaryotes [7]. Versions of the domain in prokaryotic cognates of the ubiquitin-modification pathway are shown to have a similar role, and the archaeal protein from Haloferax volcanii is found to cleave ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates [8,9].	Domain
CA [auth c], E, KA [auth k], M, SA [auth s], CA [auth c], E, KA [auth k], M, SA [auth s], U	PF18392	COP9 signalosome complex subunit 7a helix I domain (CSN7a_helixI)	COP9 signalosome complex subunit 7a helix I domain	This is The C-terminal helix I domain found in COP9 signalosome complex subunit 7a. The helix from CSN7 (helix I) contacts CSN6 helices I and II at the base of the bundle, nearest the PCI ring [1].	Domain
CA [auth c], E, KA [auth k], M, SA [auth s], CA [auth c], E, KA [auth k], M, SA [auth s], U	PF01399	PCI domain (PCI)	PCI domain	This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].	Domain
BA [auth b], D, JA [auth j], L, RA [auth r], BA [auth b], D, JA [auth j], L, RA [auth r], T	PF22241	PSMD12/CSN4, N-terminal (PSMD12-CSN4_N)	PSMD12/CSN4, N-terminal	-	Repeat
BA [auth b], D, JA [auth j], L, RA [auth r], BA [auth b], D, JA [auth j], L, RA [auth r], T	PF18420	CSN4/RPN5/eIF3a helix turn helix domain (CSN4_RPN5_eIF3a)	CSN4/RPN5/eIF3a helix turn helix domain	Cullin-RING E3 ubiquitin ligases (CRLs) are regulated by the eight-subunit COP9 signalosome (CSN). Enzymatically, CSN functions as an isopeptidase that removes the ubiquitin-like activator NEDD8 from CRLs, but it can also bind deneddylated CRLs and m ...	Cullin-RING E3 ubiquitin ligases (CRLs) are regulated by the eight-subunit COP9 signalosome (CSN). Enzymatically, CSN functions as an isopeptidase that removes the ubiquitin-like activator NEDD8 from CRLs, but it can also bind deneddylated CRLs and maintain them in an inactive state. The CSN subunits CSN1, CSN2, CSN3, CSN4, CSN7 and CSN8, share a common domain composition: an N-terminal array of tandem alpha-helical tetratricopeptide/-like repeats, a 34 residue motif, followed by a PCI domain, which encompasses a WH subdomain, a linker, and one or two alpha-helices at the C-terminus. This entry describes the C-terminal helices found on CSN4. The two helices from CSN4 (helices I and II) form a brace roughly perpendicular to the bundle axis in contact with the three C-terminal helices of CSN6. CSN5, whose two C-terminal helices form an antiparallel hairpin, inserts its final C-terminal helix (helix II) into the central CSN6 framework at the core of the bundle. Both CSN1 and CSN4 are dependent on the presence of their C-terminal helix (CSN1 isoform-2 residues: 466-527; and CSN4: 364-406) for integration into CSN. COP9 signalosome shares common architecture with the 26S proteasome lid and eIF3 where the 19S lid subunit RPN5 and the eIF3 core subunit eIF3a share significant structural similarity with CSN4 [1].	Domain
BA [auth b], D, JA [auth j], L, RA [auth r], BA [auth b], D, JA [auth j], L, RA [auth r], T	PF13012	Maintenance of mitochondrial structure and function (MitMem_reg)	Maintenance of mitochondrial structure and function	-	Family
BA [auth b], D, JA [auth j], L, RA [auth r], BA [auth b], D, JA [auth j], L, RA [auth r], T	PF01398	JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)	JAB1/Mov34/MPN/PAD-1 ubiquitin protease	Proteins with this domain are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This domain is known as the MPN domain [3] and PAD-1-like domain [4], JABP1 domain [5] or J ...	Proteins with this domain are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This domain is known as the MPN domain [3] and PAD-1-like domain [4], JABP1 domain [5] or JAMM domain [7]. These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signalling and protein turnover pathways in eukaryotes [7]. Versions of the domain in prokaryotic cognates of the ubiquitin-modification pathway are shown to have a similar role, and the archaeal protein from Haloferax volcanii is found to cleave ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates [8,9].	Domain
BA [auth b], D, JA [auth j], L, RA [auth r], BA [auth b], D, JA [auth j], L, RA [auth r], T	PF01399	PCI domain (PCI)	PCI domain	This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].	Domain
AA [auth a], C, IA [auth i], K, QA [auth q], AA [auth a], C, IA [auth i], K, QA [auth q], S	PF18323	Cop9 signalosome subunit 5 C-terminal domain (CSN5_C)	Cop9 signalosome subunit 5 C-terminal domain	The COP9 (Constitutive photomorphogenesis 9) signalosome (CSN), a large multiprotein complex that resembles the 19S lid of the 26S proteasome, plays a central role in the regulation of the E3-cullin RING ubiquitin ligases (CRLs) [1]. The catalytic ac ...	The COP9 (Constitutive photomorphogenesis 9) signalosome (CSN), a large multiprotein complex that resembles the 19S lid of the 26S proteasome, plays a central role in the regulation of the E3-cullin RING ubiquitin ligases (CRLs) [1]. The catalytic activity of the CSN complex is carried by subunit 5 (CSN5), also known as c-Jun activation domain-binding protein-1 (Jab1) [1]. This entry is the C-terminal domain found in CSN5 proteins. CSN5, whose two C-terminal helices form an antiparallel hairpin, inserts its final C-terminal helix (helix II) into the central CSN6 framework at the core of the bundle. Deletion of the C-terminal helices has a pronounced effect on CSN integrity [2].	Domain
AA [auth a], C, IA [auth i], K, QA [auth q], AA [auth a], C, IA [auth i], K, QA [auth q], S	PF01398	JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)	JAB1/Mov34/MPN/PAD-1 ubiquitin protease	Proteins with this domain are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This domain is known as the MPN domain [3] and PAD-1-like domain [4], JABP1 domain [5] or J ...	Proteins with this domain are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This domain is known as the MPN domain [3] and PAD-1-like domain [4], JABP1 domain [5] or JAMM domain [7]. These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signalling and protein turnover pathways in eukaryotes [7]. Versions of the domain in prokaryotic cognates of the ubiquitin-modification pathway are shown to have a similar role, and the archaeal protein from Haloferax volcanii is found to cleave ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates [8,9].	Domain
AA [auth a], C, IA [auth i], K, QA [auth q], AA [auth a], C, IA [auth i], K, QA [auth q], S	PF22788	COP9 signalosome complex subunit 3, N-terminal helical repeats (COP9_hel_rpt)	COP9 signalosome complex subunit 3, N-terminal helical repeats	-	Repeat
AA [auth a], C, IA [auth i], K, QA [auth q], AA [auth a], C, IA [auth i], K, QA [auth q], S	PF21215	COP9 signalosome complex subunit 3-like, C-terminal helix (CSN3-like_C)	COP9 signalosome complex subunit 3-like, C-terminal helix	This domain is found in COP9 signalosome complex subunit 3 from humans (CSN3) and similar proteins predominantly found in vertebrates. CSN3 is a component of the eight-subunit COP9 signalosome complex (CSN), which inactivate Cullin-RING E3 ubiquitin ...	This domain is found in COP9 signalosome complex subunit 3 from humans (CSN3) and similar proteins predominantly found in vertebrates. CSN3 is a component of the eight-subunit COP9 signalosome complex (CSN), which inactivate Cullin-RING E3 ubiquitin ligases (CRLs) by removing their covalently attached activator, NEDD8. This entry represents the C-terminal helical decoration of this protein [1,2].	Domain
AA [auth a], C, IA [auth i], K, QA [auth q], AA [auth a], C, IA [auth i], K, QA [auth q], S	PF01399	PCI domain (PCI)	PCI domain	This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].	Domain
B, HA [auth h], J, PA [auth p], R, B, HA [auth h], J, PA [auth p], R, Z	PF22241	PSMD12/CSN4, N-terminal (PSMD12-CSN4_N)	PSMD12/CSN4, N-terminal	-	Repeat
B, HA [auth h], J, PA [auth p], R, B, HA [auth h], J, PA [auth p], R, Z	PF18420	CSN4/RPN5/eIF3a helix turn helix domain (CSN4_RPN5_eIF3a)	CSN4/RPN5/eIF3a helix turn helix domain	Cullin-RING E3 ubiquitin ligases (CRLs) are regulated by the eight-subunit COP9 signalosome (CSN). Enzymatically, CSN functions as an isopeptidase that removes the ubiquitin-like activator NEDD8 from CRLs, but it can also bind deneddylated CRLs and m ...	Cullin-RING E3 ubiquitin ligases (CRLs) are regulated by the eight-subunit COP9 signalosome (CSN). Enzymatically, CSN functions as an isopeptidase that removes the ubiquitin-like activator NEDD8 from CRLs, but it can also bind deneddylated CRLs and maintain them in an inactive state. The CSN subunits CSN1, CSN2, CSN3, CSN4, CSN7 and CSN8, share a common domain composition: an N-terminal array of tandem alpha-helical tetratricopeptide/-like repeats, a 34 residue motif, followed by a PCI domain, which encompasses a WH subdomain, a linker, and one or two alpha-helices at the C-terminus. This entry describes the C-terminal helices found on CSN4. The two helices from CSN4 (helices I and II) form a brace roughly perpendicular to the bundle axis in contact with the three C-terminal helices of CSN6. CSN5, whose two C-terminal helices form an antiparallel hairpin, inserts its final C-terminal helix (helix II) into the central CSN6 framework at the core of the bundle. Both CSN1 and CSN4 are dependent on the presence of their C-terminal helix (CSN1 isoform-2 residues: 466-527; and CSN4: 364-406) for integration into CSN. COP9 signalosome shares common architecture with the 26S proteasome lid and eIF3 where the 19S lid subunit RPN5 and the eIF3 core subunit eIF3a share significant structural similarity with CSN4 [1].	Domain
B, HA [auth h], J, PA [auth p], R, B, HA [auth h], J, PA [auth p], R, Z	PF01399	PCI domain (PCI)	PCI domain	This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].	Domain
A, GA [auth g], I, OA [auth o], Q, A, GA [auth g], I, OA [auth o], Q, Y	PF21151	COP9 signalosome complex subunit 1, C-terminal helix (CSN1_C)	COP9 signalosome complex subunit 1, C-terminal helix	This is the C-terminal helix from COP9 signalosome complex subunit 1, an essential component of the COP9 signalosome complex (CSN), which involved in various cellular and developmental processes [1,2].	Domain
A, GA [auth g], I, OA [auth o], Q, A, GA [auth g], I, OA [auth o], Q, Y	PF21215	COP9 signalosome complex subunit 3-like, C-terminal helix (CSN3-like_C)	COP9 signalosome complex subunit 3-like, C-terminal helix	This domain is found in COP9 signalosome complex subunit 3 from humans (CSN3) and similar proteins predominantly found in vertebrates. CSN3 is a component of the eight-subunit COP9 signalosome complex (CSN), which inactivate Cullin-RING E3 ubiquitin ...	This domain is found in COP9 signalosome complex subunit 3 from humans (CSN3) and similar proteins predominantly found in vertebrates. CSN3 is a component of the eight-subunit COP9 signalosome complex (CSN), which inactivate Cullin-RING E3 ubiquitin ligases (CRLs) by removing their covalently attached activator, NEDD8. This entry represents the C-terminal helical decoration of this protein [1,2].	Domain
A, GA [auth g], I, OA [auth o], Q, A, GA [auth g], I, OA [auth o], Q, Y	PF10602	26S proteasome subunit RPN7 (RPN7)	26S proteasome subunit RPN7	-	Repeat
A, GA [auth g], I, OA [auth o], Q, A, GA [auth g], I, OA [auth o], Q, Y	PF01399	PCI domain (PCI)	PCI domain	This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
FA [auth f], H, NA [auth n], P, VA [auth v], FA [auth f], H, NA [auth n], P, VA [auth v], X	COP9 signalosome complex subunit 8	-	cellular response to stimulus regulation of cellular process positive regulation of phosphorylation response to stimulus regulation of catalytic activity regulation of transferase activity positive regulation of phosphate metabolic process intracellular signal transduction regulation of primary metabolic process cell communication positive regulation of metabolic process phosphate-containing compound metabolic process intracellular signaling cassette positive regulation of macromolecule metabolic process cellular response to stimulus regulation of cellular process positive regulation of phosphorylation response to stimulus regulation of catalytic activity regulation of transferase activity positive regulation of phosphate metabolic process intracellular signal transduction regulation of primary metabolic process cell communication positive regulation of metabolic process phosphate-containing compound metabolic process intracellular signaling cassette positive regulation of macromolecule metabolic process signal transduction phosphorus metabolic process protein modification process positive regulation of protein phosphorylation activation of NF-kappaB-inducing kinase activity regulation of biological process protein phosphorylation positive regulation of phosphorus metabolic process phosphorylation non-canonical NF-kappaB signal transduction regulation of protein metabolic process primary metabolic process regulation of molecular function positive regulation of kinase activity regulation of kinase activity activation of protein kinase activity macromolecule modification regulation of phosphorus metabolic process metabolic process macromolecule metabolic process regulation of metabolic process regulation of protein modification process regulation of protein phosphorylation signaling positive regulation of protein metabolic process positive regulation of biological process positive regulation of molecular function positive regulation of protein modification process protein metabolic process positive regulation of protein kinase activity positive regulation of cellular process biological regulation positive regulation of catalytic activity regulation of protein kinase activity regulation of macromolecule metabolic process regulation of phosphorylation cellular process cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization COP9 signalosome assembly protein-containing complex assembly cellular component organization or biogenesis negative regulation of cell population proliferation cell population proliferation regulation of cell population proliferation negative regulation of cellular process negative regulation of biological process post-translational protein modification protein neddylation protein modification by small protein conjugation protein modification by small protein conjugation or removal protein deneddylation protein modification by small protein removal regulation of post-translational protein modification regulation of protein neddylation regulation of protein modification by small protein conjugation or removal	extracellular exosome membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol perinuclear region of cytoplasm extracellular exosome membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol perinuclear region of cytoplasm intracellular organelle protein-containing complex nucleus nuclear protein-containing complex COP9 signalosome intracellular membrane-bounded organelle membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen
EA [auth e], G, MA [auth m], O, UA [auth u], EA [auth e], G, MA [auth m], O, UA [auth u], W	COP9 signalosome complex subunit 7a	-	primary metabolic process macromolecule modification metabolic process cellular process protein metabolic process macromolecule metabolic process post-translational protein modification protein modification process protein neddylation protein modification by small protein conjugation protein modification by small protein conjugation or removal protein deneddylation protein modification by small protein removal cellular component organization primary metabolic process macromolecule modification metabolic process cellular process protein metabolic process macromolecule metabolic process post-translational protein modification protein modification process protein neddylation protein modification by small protein conjugation protein modification by small protein conjugation or removal protein deneddylation protein modification by small protein removal cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization COP9 signalosome assembly protein-containing complex assembly cellular component organization or biogenesis regulation of biological process regulation of cellular process regulation of protein modification process regulation of post-translational protein modification regulation of protein metabolic process biological regulation regulation of macromolecule metabolic process regulation of primary metabolic process regulation of protein neddylation regulation of protein modification by small protein conjugation or removal regulation of metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle protein-containing complex organelle nucleus nuclear protein-containing complex COP9 signalosome intracellular membrane-bounded organelle membrane-enclosed lumen intracellular organelle lumen cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle protein-containing complex organelle nucleus nuclear protein-containing complex COP9 signalosome intracellular membrane-bounded organelle membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen
DA [auth d], F, LA [auth l], N, TA [auth t], DA [auth d], F, LA [auth l], N, TA [auth t], V	COP9 signalosome complex subunit 6	-	primary metabolic process macromolecule modification metabolic process cellular process protein metabolic process macromolecule metabolic process post-translational protein modification protein modification process protein neddylation protein modification by small protein conjugation protein modification by small protein conjugation or removal protein deneddylation protein modification by small protein removal regulation of biological process primary metabolic process macromolecule modification metabolic process cellular process protein metabolic process macromolecule metabolic process post-translational protein modification protein modification process protein neddylation protein modification by small protein conjugation protein modification by small protein conjugation or removal protein deneddylation protein modification by small protein removal regulation of biological process regulation of cellular process regulation of protein modification process regulation of post-translational protein modification regulation of protein metabolic process biological regulation regulation of macromolecule metabolic process regulation of primary metabolic process regulation of protein neddylation regulation of protein modification by small protein conjugation or removal regulation of metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol perinuclear region of cytoplasm membrane-bounded organelle intracellular organelle protein-containing complex organelle nucleus nuclear protein-containing complex COP9 signalosome intracellular membrane-bounded organelle membrane-enclosed lumen cellular anatomical structure intracellular anatomical structure cytoplasm cytosol perinuclear region of cytoplasm membrane-bounded organelle intracellular organelle protein-containing complex organelle nucleus nuclear protein-containing complex COP9 signalosome intracellular membrane-bounded organelle membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen
CA [auth c], E, KA [auth k], M, SA [auth s], CA [auth c], E, KA [auth k], M, SA [auth s], U	COP9 signalosome complex subunit 5	translation factor activity translation initiation factor activity peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity ubiquitin-like protein peptidase activity deNEDDylase activity transcription coactivator activity transcription regulator activity transcription coregulator activity protein-macromolecule adaptor activity molecular adaptor activity translation factor activity translation initiation factor activity peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity ubiquitin-like protein peptidase activity deNEDDylase activity transcription coactivator activity transcription regulator activity transcription coregulator activity protein-macromolecule adaptor activity molecular adaptor activity metal-dependent deubiquitinase activity deubiquitinase activity protein binding binding enzyme binding macrophage migration inhibitory factor binding cytokine binding cation binding ion binding metal ion binding small molecule binding	cellular response to stimulus regulation of cellular process response to stimulus signaling regulation of cellular response to stress endoplasmic reticulum unfolded protein response regulation of response to endoplasmic reticulum stress regulation of signal transduction intracellular signal transduction cell communication regulation of endoplasmic reticulum unfolded protein response cellular response to stress regulation of intracellular signal transduction response to stress regulation of response to stress cellular response to stimulus regulation of cellular process response to stimulus signaling regulation of cellular response to stress endoplasmic reticulum unfolded protein response regulation of response to endoplasmic reticulum stress regulation of signal transduction intracellular signal transduction cell communication regulation of endoplasmic reticulum unfolded protein response cellular response to stress regulation of intracellular signal transduction response to stress regulation of response to stress signal transduction regulation of IRE1-mediated unfolded protein response response to endoplasmic reticulum stress regulation of biological process regulation of signaling cellular response to topologically incorrect protein biological regulation cellular response to unfolded protein response to unfolded protein regulation of response to stimulus response to topologically incorrect protein IRE1-mediated unfolded protein response regulation of cell communication cellular process regulation of JNK cascade regulation of MAPK cascade JNK cascade intracellular signaling cassette MAPK cascade negative regulation of programmed cell death regulation of apoptotic process negative regulation of biological process regulation of programmed cell death cell death negative regulation of apoptotic process negative regulation of cellular process apoptotic process programmed cell death positive regulation of DNA-binding transcription factor activity RNA metabolic process regulation of primary metabolic process nucleobase-containing compound metabolic process RNA biosynthetic process positive regulation of molecular function nucleic acid biosynthetic process DNA-templated transcription regulation of RNA metabolic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of biosynthetic process primary metabolic process regulation of macromolecule metabolic process nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process nucleic acid metabolic process regulation of molecular function regulation of gene expression biosynthetic process regulation of DNA-binding transcription factor activity metabolic process regulation of macromolecule biosynthetic process regulation of DNA-templated transcription macromolecule metabolic process regulation of metabolic process macromolecule modification protein metabolic process post-translational protein modification protein modification process protein neddylation protein modification by small protein conjugation protein modification by small protein conjugation or removal regulation of protein modification process regulation of post-translational protein modification regulation of protein metabolic process regulation of protein neddylation regulation of protein modification by small protein conjugation or removal cell cycle regulation of cell cycle protein deneddylation protein modification by small protein removal exosomal secretion vesicle localization establishment of organelle localization cellular localization transport secretion establishment of vesicle localization export from cell establishment of localization extracellular exosome biogenesis vesicle-mediated transport cellular component biogenesis localization secretion by cell exocytosis extracellular vesicle biogenesis organelle localization establishment of localization in cell cellular component organization or biogenesis proteolysis positive regulation of DNA-templated transcription positive regulation of biological process positive regulation of macromolecule biosynthetic process positive regulation of metabolic process transcription by RNA polymerase II positive regulation of biosynthetic process positive regulation of macromolecule metabolic process positive regulation of cellular process regulation of transcription by RNA polymerase II positive regulation of transcription by RNA polymerase II positive regulation of RNA metabolic process positive regulation of RNA biosynthetic process translation protein biosynthetic process	eukaryotic translation initiation factor 3 complex protein-containing complex cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle organelle nucleus nuclear protein-containing complex COP9 signalosome intracellular membrane-bounded organelle membrane-enclosed lumen eukaryotic translation initiation factor 3 complex protein-containing complex cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle organelle nucleus nuclear protein-containing complex COP9 signalosome intracellular membrane-bounded organelle membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen membraneless organelle intracellular membraneless organelle chromatin chromosome perinuclear region of cytoplasm transport vesicle synapse intracellular vesicle endomembrane system presynapse cytoplasmic vesicle synaptic vesicle cell junction secretory vesicle vesicle exocytic vesicle
BA [auth b], D, JA [auth j], L, RA [auth r], BA [auth b], D, JA [auth j], L, RA [auth r], T	COP9 signalosome complex subunit 4	ubiquitin-like protein peptidase activity peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity deNEDDylase activity	primary metabolic process macromolecule modification metabolic process cellular process protein metabolic process macromolecule metabolic process post-translational protein modification protein modification process protein neddylation protein modification by small protein conjugation protein modification by small protein conjugation or removal protein deneddylation protein modification by small protein removal regulation of biological process primary metabolic process macromolecule modification metabolic process cellular process protein metabolic process macromolecule metabolic process post-translational protein modification protein modification process protein neddylation protein modification by small protein conjugation protein modification by small protein conjugation or removal protein deneddylation protein modification by small protein removal regulation of biological process regulation of cellular process regulation of protein modification process regulation of post-translational protein modification regulation of protein metabolic process biological regulation regulation of macromolecule metabolic process regulation of primary metabolic process regulation of protein neddylation regulation of protein modification by small protein conjugation or removal regulation of metabolic process	cellular anatomical structure cell junction membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membraneless organelle intracellular membrane-bounded organelle intracellular organelle lumen nuclear speck ribonucleoprotein granule intracellular organelle nuclear body nucleoplasm cellular anatomical structure cell junction membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membraneless organelle intracellular membrane-bounded organelle intracellular organelle lumen nuclear speck ribonucleoprotein granule intracellular organelle nuclear body nucleoplasm organelle lumen organelle membraneless organelle supramolecular complex nuclear ribonucleoprotein granule nuclear lumen cytoplasm cytosol protein-containing complex nuclear protein-containing complex COP9 signalosome transport vesicle synapse intracellular vesicle endomembrane system presynapse cytoplasmic vesicle synaptic vesicle secretory vesicle vesicle exocytic vesicle
AA [auth a], C, IA [auth i], K, QA [auth q], AA [auth a], C, IA [auth i], K, QA [auth q], S	COP9 signalosome complex subunit 3	-	catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process cellular process macromolecule metabolic process protein metabolic process response to light stimulus catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process cellular process macromolecule metabolic process protein metabolic process response to light stimulus response to stimulus response to radiation response to abiotic stimulus macromolecule modification post-translational protein modification protein modification process protein neddylation protein modification by small protein conjugation protein modification by small protein conjugation or removal protein deneddylation protein modification by small protein removal cellular response to stimulus regulation of cellular process signaling regulation of cellular response to stress regulation of signal transduction DNA damage response, signal transduction by p53 class mediator intracellular signal transduction cell communication cellular response to stress regulation of intracellular signal transduction response to stress regulation of response to stress regulation of signal transduction by p53 class mediator signal transduction regulation of DNA damage response, signal transduction by p53 class mediator regulation of biological process regulation of signaling biological regulation signal transduction by p53 class mediator regulation of response to stimulus DNA damage response regulation of cell communication signal transduction in response to DNA damage regulation of protein modification process regulation of post-translational protein modification regulation of protein metabolic process regulation of macromolecule metabolic process regulation of primary metabolic process regulation of protein neddylation regulation of protein modification by small protein conjugation or removal regulation of metabolic process developmental process multicellular organism development multicellular organismal process embryo development ending in birth or egg hatching chordate embryonic development anatomical structure development embryo development in utero embryonic development	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol perinuclear region of cytoplasm membrane-bounded organelle intracellular organelle protein-containing complex organelle nucleus nuclear protein-containing complex COP9 signalosome intracellular membrane-bounded organelle membrane-enclosed lumen cellular anatomical structure intracellular anatomical structure cytoplasm cytosol perinuclear region of cytoplasm membrane-bounded organelle intracellular organelle protein-containing complex organelle nucleus nuclear protein-containing complex COP9 signalosome intracellular membrane-bounded organelle membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen
B, HA [auth h], J, PA [auth p], R, B, HA [auth h], J, PA [auth p], R, Z	COP9 signalosome complex subunit 2	transcription corepressor activity transcription regulator activity transcription coregulator activity protein-macromolecule adaptor activity molecular adaptor activity	developmental process multicellular organismal process cell population proliferation developmental growth chordate embryonic development growth embryo development trophectodermal cell proliferation in utero embryonic development multicellular organism development embryo development ending in birth or egg hatching anatomical structure development cellular process blastocyst growth developmental process multicellular organismal process cell population proliferation developmental growth chordate embryonic development growth embryo development trophectodermal cell proliferation in utero embryonic development multicellular organism development embryo development ending in birth or egg hatching anatomical structure development cellular process blastocyst growth blastocyst development protein phosphorylation phosphorylation primary metabolic process macromolecule modification phosphate-containing compound metabolic process metabolic process protein metabolic process macromolecule metabolic process protein modification process phosphorus metabolic process RNA metabolic process nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process DNA-templated transcription nucleic acid biosynthetic process transcription by RNA polymerase II biosynthetic process post-translational protein modification protein neddylation protein modification by small protein conjugation protein modification by small protein conjugation or removal regulation of cellular process negative regulation of biological process regulation of primary metabolic process negative regulation of RNA biosynthetic process regulation of RNA metabolic process negative regulation of cellular process negative regulation of nucleobase-containing compound metabolic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process negative regulation of macromolecule metabolic process regulation of biosynthetic process regulation of transcription by RNA polymerase II negative regulation of DNA-templated transcription regulation of biological process negative regulation of transcription by RNA polymerase II negative regulation of metabolic process biological regulation regulation of macromolecule metabolic process regulation of gene expression negative regulation of biosynthetic process negative regulation of macromolecule biosynthetic process regulation of macromolecule biosynthetic process regulation of DNA-templated transcription regulation of metabolic process negative regulation of RNA metabolic process protein deneddylation protein modification by small protein removal cellular developmental process nervous system development generation of neurons neurogenesis neuron differentiation cell differentiation system development regulation of protein modification process regulation of post-translational protein modification regulation of protein metabolic process regulation of protein neddylation regulation of protein modification by small protein conjugation or removal skeletal muscle cell differentiation skeletal muscle tissue development animal organ development tissue development striated muscle tissue development muscle structure development skeletal muscle organ development muscle tissue development muscle organ development cellular response to stimulus response to stimulus signaling signal transduction cell communication inner cell mass cell proliferation	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle protein-containing complex organelle nucleus nuclear protein-containing complex COP9 signalosome intracellular membrane-bounded organelle membrane-enclosed lumen intracellular organelle lumen cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle protein-containing complex organelle nucleus nuclear protein-containing complex COP9 signalosome intracellular membrane-bounded organelle membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen
A, GA [auth g], I, OA [auth o], Q, A, GA [auth g], I, OA [auth o], Q, Y	COP9 signalosome complex subunit 1	GTPase regulator activity enzyme regulator activity GTPase inhibitor activity molecular function inhibitor activity nucleoside-triphosphatase regulator activity molecular function regulator activity enzyme inhibitor activity	cellular response to stimulus regulation of biological process regulation of cellular process response to stimulus signaling biological regulation intracellular signal transduction cell communication JNK cascade intracellular signaling cassette MAPK cascade cellular process signal transduction primary metabolic process cellular response to stimulus regulation of biological process regulation of cellular process response to stimulus signaling biological regulation intracellular signal transduction cell communication JNK cascade intracellular signaling cassette MAPK cascade cellular process signal transduction primary metabolic process macromolecule modification metabolic process protein metabolic process macromolecule metabolic process post-translational protein modification protein modification process protein neddylation protein modification by small protein conjugation protein modification by small protein conjugation or removal protein deneddylation protein modification by small protein removal regulation of protein modification process regulation of post-translational protein modification regulation of protein metabolic process regulation of macromolecule metabolic process regulation of primary metabolic process regulation of protein neddylation regulation of protein modification by small protein conjugation or removal regulation of metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle protein-containing complex organelle nucleus nuclear protein-containing complex COP9 signalosome intracellular membrane-bounded organelle membrane-enclosed lumen intracellular organelle lumen cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle protein-containing complex organelle nucleus nuclear protein-containing complex COP9 signalosome intracellular membrane-bounded organelle membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
FA [auth f], H, NA [auth n], P, VA [auth v], FA [auth f], H, NA [auth n], P, VA [auth v], X	IPR033205	COP9 signalosome, subunit CSN8	Family
FA [auth f], H, NA [auth n], P, VA [auth v], FA [auth f], H, NA [auth n], P, VA [auth v], X	IPR033464	CSN8/PSMD8/EIF3K	Domain
FA [auth f], H, NA [auth n], P, VA [auth v], FA [auth f], H, NA [auth n], P, VA [auth v], X	IPR000717	Proteasome component (PCI) domain	Domain
EA [auth e], G, MA [auth m], O, UA [auth u], EA [auth e], G, MA [auth m], O, UA [auth u], W	IPR045237	Eukaryotic translation initiation factor 3 subunit M eIF3m/COP9 signalosome complex subunit 7 COPS7	Family
EA [auth e], G, MA [auth m], O, UA [auth u], EA [auth e], G, MA [auth m], O, UA [auth u], W	IPR041481	COP9 signalosome complex subunit 7, helix I	Domain
EA [auth e], G, MA [auth m], O, UA [auth u], EA [auth e], G, MA [auth m], O, UA [auth u], W	IPR000717	Proteasome component (PCI) domain	Domain
DA [auth d], F, LA [auth l], N, TA [auth t], DA [auth d], F, LA [auth l], N, TA [auth t], V	IPR024969	EIF3F/CSN6-like, C-terminal	Domain
DA [auth d], F, LA [auth l], N, TA [auth t], DA [auth d], F, LA [auth l], N, TA [auth t], V	IPR037518	MPN domain	Domain
DA [auth d], F, LA [auth l], N, TA [auth t], DA [auth d], F, LA [auth l], N, TA [auth t], V	IPR033859	COP9 signalosome subunit 6	Family
DA [auth d], F, LA [auth l], N, TA [auth t], DA [auth d], F, LA [auth l], N, TA [auth t], V	IPR000555	JAB1/MPN/MOV34 metalloenzyme domain	Domain
CA [auth c], E, KA [auth k], M, SA [auth s], CA [auth c], E, KA [auth k], M, SA [auth s], U	IPR040961	Cop9 signalosome subunit 5 C-terminal domain	Domain
CA [auth c], E, KA [auth k], M, SA [auth s], CA [auth c], E, KA [auth k], M, SA [auth s], U	IPR050242	JAMM/MPN+ metalloenzymes, peptidase M67A	Family
CA [auth c], E, KA [auth k], M, SA [auth s], CA [auth c], E, KA [auth k], M, SA [auth s], U	IPR037518	MPN domain	Domain
CA [auth c], E, KA [auth k], M, SA [auth s], CA [auth c], E, KA [auth k], M, SA [auth s], U	IPR000555	JAB1/MPN/MOV34 metalloenzyme domain	Domain
BA [auth b], D, JA [auth j], L, RA [auth r], BA [auth b], D, JA [auth j], L, RA [auth r], T	IPR041406	COP9 signalosome complex subunit 4, helix turn helix domain	Domain
BA [auth b], D, JA [auth j], L, RA [auth r], BA [auth b], D, JA [auth j], L, RA [auth r], T	IPR036388	Winged helix-like DNA-binding domain superfamily	Homologous Superfamily
BA [auth b], D, JA [auth j], L, RA [auth r], BA [auth b], D, JA [auth j], L, RA [auth r], T	IPR036390	Winged helix DNA-binding domain superfamily	Homologous Superfamily
BA [auth b], D, JA [auth j], L, RA [auth r], BA [auth b], D, JA [auth j], L, RA [auth r], T	IPR000717	Proteasome component (PCI) domain	Domain
BA [auth b], D, JA [auth j], L, RA [auth r], BA [auth b], D, JA [auth j], L, RA [auth r], T	IPR040134	26S Proteasome non-ATPase regulatory subunit 12/COP9 signalosome complex subunit 4	Family
BA [auth b], D, JA [auth j], L, RA [auth r], BA [auth b], D, JA [auth j], L, RA [auth r], T	IPR054559	PSMD12/CSN4-like, N-terminal	Domain
AA [auth a], C, IA [auth i], K, QA [auth q], AA [auth a], C, IA [auth i], K, QA [auth q], S	IPR048621	COP9 signalosome complex subunit 3, C-terminal helix	Domain
AA [auth a], C, IA [auth i], K, QA [auth q], AA [auth a], C, IA [auth i], K, QA [auth q], S	IPR050756	COP9 signalosome complex subunit 3	Family
AA [auth a], C, IA [auth i], K, QA [auth q], AA [auth a], C, IA [auth i], K, QA [auth q], S	IPR036390	Winged helix DNA-binding domain superfamily	Homologous Superfamily
AA [auth a], C, IA [auth i], K, QA [auth q], AA [auth a], C, IA [auth i], K, QA [auth q], S	IPR055089	COP9 signalosome complex subunit 3, N-terminal helical repeats	Domain
AA [auth a], C, IA [auth i], K, QA [auth q], AA [auth a], C, IA [auth i], K, QA [auth q], S	IPR000717	Proteasome component (PCI) domain	Domain
B, HA [auth h], J, PA [auth p], R, B, HA [auth h], J, PA [auth p], R, Z	IPR050871	26S Proteasome and COP9 Signalosome Components	Family
B, HA [auth h], J, PA [auth p], R, B, HA [auth h], J, PA [auth p], R, Z	IPR011990	Tetratricopeptide-like helical domain superfamily	Homologous Superfamily
B, HA [auth h], J, PA [auth p], R, B, HA [auth h], J, PA [auth p], R, Z	IPR036390	Winged helix DNA-binding domain superfamily	Homologous Superfamily
B, HA [auth h], J, PA [auth p], R, B, HA [auth h], J, PA [auth p], R, Z	IPR000717	Proteasome component (PCI) domain	Domain
A, GA [auth g], I, OA [auth o], Q, A, GA [auth g], I, OA [auth o], Q, Y	IPR048624	COP9 signalosome complex subunit 1, C-terminal helix	Domain
A, GA [auth g], I, OA [auth o], Q, A, GA [auth g], I, OA [auth o], Q, Y	IPR019585	26S proteasome regulatory subunit Rpn7/COP9 signalosome complex subunit 1	Family
A, GA [auth g], I, OA [auth o], Q, A, GA [auth g], I, OA [auth o], Q, Y	IPR036390	Winged helix DNA-binding domain superfamily	Homologous Superfamily
A, GA [auth g], I, OA [auth o], Q, A, GA [auth g], I, OA [auth o], Q, Y	IPR000717	Proteasome component (PCI) domain	Domain
A, GA [auth g], I, OA [auth o], Q, A, GA [auth g], I, OA [auth o], Q, Y	IPR045135	26S proteasome regulatory subunit Rpn7, N-terminal	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
FA [auth f], H, NA [auth n], P, VA [auth v], FA [auth f], H, NA [auth n], P, VA [auth v], X	Pharos: Q99627	Alzheimer disease glioblastoma lung cancer malignant mesothelioma myopathy ovarian cancer primitive neuroectodermal tumor astrocytic tumor heart disease malignant ependymoma malignant pancreatic neoplasm oligodendroglioma Pick disease atypical teratoid rhabdoid tumor large cell medulloblastoma Alzheimer disease glioblastoma lung cancer malignant mesothelioma myopathy ovarian cancer primitive neuroectodermal tumor astrocytic tumor heart disease malignant ependymoma malignant pancreatic neoplasm oligodendroglioma Pick disease atypical teratoid rhabdoid tumor large cell medulloblastoma malignant glioma medulloblastoma osteosarcoma pilocytic astrocytoma
EA [auth e], G, MA [auth m], O, UA [auth u], EA [auth e], G, MA [auth m], O, UA [auth u], W	Pharos: Q9UBW8	Disease Exacerbation gastric neoplasm medulloblastoma hereditary diffuse gastric adenocarcinoma ovarian cancer gastric cancer psoriasis
DA [auth d], F, LA [auth l], N, TA [auth t], DA [auth d], F, LA [auth l], N, TA [auth t], V	Pharos: Q7L5N1	HIV infectious disease chronic obstructive pulmonary disease idiopathic pulmonary fibrosis HIV Coinfection ovarian cancer plasma cell myeloma
CA [auth c], E, KA [auth k], M, SA [auth s], CA [auth c], E, KA [auth k], M, SA [auth s], U	Pharos: Q92905	Stevens-Johnson syndrome brain aneurysm Liver carcinoma medulloblastoma plasma cell myeloma lymphoplasmacytic lymphoma psoriasis toxic epidermal necrolysis hepatocellular carcinoma Machado-Joseph disease ovarian cancer
BA [auth b], D, JA [auth j], L, RA [auth r], BA [auth b], D, JA [auth j], L, RA [auth r], T	Pharos: Q9BT78	diabetes mellitus malignant colon neoplasm lung carcinoma ovarian cancer lymphoplasmacytic lymphoma plasma cell myeloma
AA [auth a], C, IA [auth i], K, QA [auth q], AA [auth a], C, IA [auth i], K, QA [auth q], S	Pharos: Q9UNS2	Hepatomegaly plasma cell myeloma osteosarcoma ovarian cancer
B, HA [auth h], J, PA [auth p], R, B, HA [auth h], J, PA [auth p], R, Z	Pharos: P61201	endometriosis Endometrioma lung adenocarcinoma plasma cell myeloma lymphoplasmacytic lymphoma tuberculosis hereditary spastic paraplegia ovarian cancer
A, GA [auth g], I, OA [auth o], Q, A, GA [auth g], I, OA [auth o], Q, Y	Pharos: Q13098	attention deficit hyperactivity disorder, inattentive type malignant mesothelioma schizophrenia