9UNW

mouse PDCD5-TRiC complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001669	cellular_component	acrosomal vesicle
A	0002199	cellular_component	zona pellucida receptor complex
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005832	cellular_component	chaperonin-containing T-complex
A	0005874	cellular_component	microtubule
A	0006457	biological_process	protein folding
A	0007339	biological_process	binding of sperm to zona pellucida
A	0016887	molecular_function	ATP hydrolysis activity
A	0032212	biological_process	positive regulation of telomere maintenance via telomerase
A	0044183	molecular_function	protein folding chaperone
A	0044297	cellular_component	cell body
A	0050821	biological_process	protein stabilization
A	0071987	molecular_function	WD40-repeat domain binding
A	1904851	biological_process	positive regulation of establishment of protein localization to telomere
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005832	cellular_component	chaperonin-containing T-complex
B	0005874	cellular_component	microtubule
B	0006457	biological_process	protein folding
B	0007339	biological_process	binding of sperm to zona pellucida
B	0016887	molecular_function	ATP hydrolysis activity
B	0032212	biological_process	positive regulation of telomere maintenance via telomerase
B	0042802	molecular_function	identical protein binding
B	0044183	molecular_function	protein folding chaperone
B	0044297	cellular_component	cell body
B	0050821	biological_process	protein stabilization
C	0000242	cellular_component	pericentriolar material
C	0000792	cellular_component	heterochromatin
C	0001669	cellular_component	acrosomal vesicle
C	0002199	cellular_component	zona pellucida receptor complex
C	0005515	molecular_function	protein binding
C	0005794	cellular_component	Golgi apparatus
C	0005813	cellular_component	centrosome
C	0005815	cellular_component	microtubule organizing center
C	0005829	cellular_component	cytosol
C	0005832	cellular_component	chaperonin-containing T-complex
C	0005874	cellular_component	microtubule
C	0006457	biological_process	protein folding
C	0007339	biological_process	binding of sperm to zona pellucida
C	0016887	molecular_function	ATP hydrolysis activity
C	0031625	molecular_function	ubiquitin protein ligase binding
C	0032212	biological_process	positive regulation of telomere maintenance via telomerase
C	0043209	cellular_component	myelin sheath
C	0044183	molecular_function	protein folding chaperone
C	0044297	cellular_component	cell body
C	0050821	biological_process	protein stabilization
C	0090666	biological_process	scaRNA localization to Cajal body
C	0140535	cellular_component	intracellular protein-containing complex
C	1904851	biological_process	positive regulation of establishment of protein localization to telomere
C	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006915	biological_process	apoptotic process
D	0008201	molecular_function	heparin binding
D	0010628	biological_process	positive regulation of gene expression
D	0010698	molecular_function	acetyltransferase activator activity
D	0042110	biological_process	T cell activation
D	0042981	biological_process	regulation of apoptotic process
D	0043065	biological_process	positive regulation of apoptotic process
D	0048487	molecular_function	beta-tubulin binding
D	0071560	biological_process	cellular response to transforming growth factor beta stimulus
D	0140311	molecular_function	protein sequestering activity
D	1901798	biological_process	positive regulation of signal transduction by p53 class mediator
D	1902255	biological_process	positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator
D	1903333	biological_process	negative regulation of protein folding
E	0002199	cellular_component	zona pellucida receptor complex
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005813	cellular_component	centrosome
E	0005829	cellular_component	cytosol
E	0005832	cellular_component	chaperonin-containing T-complex
E	0005874	cellular_component	microtubule
E	0006457	biological_process	protein folding
E	0007339	biological_process	binding of sperm to zona pellucida
E	0016887	molecular_function	ATP hydrolysis activity
E	0032212	biological_process	positive regulation of telomere maintenance via telomerase
E	0044183	molecular_function	protein folding chaperone
E	0044297	cellular_component	cell body
E	0050821	biological_process	protein stabilization
F	0003730	molecular_function	mRNA 3'-UTR binding
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005813	cellular_component	centrosome
F	0005832	cellular_component	chaperonin-containing T-complex
F	0005874	cellular_component	microtubule
F	0006457	biological_process	protein folding
F	0007339	biological_process	binding of sperm to zona pellucida
F	0009615	biological_process	response to virus
F	0016887	molecular_function	ATP hydrolysis activity
F	0031681	molecular_function	G-protein beta-subunit binding
F	0032212	biological_process	positive regulation of telomere maintenance via telomerase
F	0043209	cellular_component	myelin sheath
F	0044183	molecular_function	protein folding chaperone
F	0044297	cellular_component	cell body
F	0048027	molecular_function	mRNA 5'-UTR binding
F	0048487	molecular_function	beta-tubulin binding
F	0050821	biological_process	protein stabilization
G	0002199	cellular_component	zona pellucida receptor complex
G	0005515	molecular_function	protein binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0005832	cellular_component	chaperonin-containing T-complex
G	0005874	cellular_component	microtubule
G	0006457	biological_process	protein folding
G	0007339	biological_process	binding of sperm to zona pellucida
G	0016887	molecular_function	ATP hydrolysis activity
G	0031625	molecular_function	ubiquitin protein ligase binding
G	0032212	biological_process	positive regulation of telomere maintenance via telomerase
G	0043209	cellular_component	myelin sheath
G	0044183	molecular_function	protein folding chaperone
G	0044297	cellular_component	cell body
G	0050821	biological_process	protein stabilization
G	0051131	biological_process	chaperone-mediated protein complex assembly
G	0090666	biological_process	scaRNA localization to Cajal body
G	0097225	cellular_component	sperm midpiece
G	0120212	cellular_component	sperm head-tail coupling apparatus
G	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
H	0002199	cellular_component	zona pellucida receptor complex
H	0005515	molecular_function	protein binding
H	0005737	cellular_component	cytoplasm
H	0005832	cellular_component	chaperonin-containing T-complex
H	0005874	cellular_component	microtubule
H	0006457	biological_process	protein folding
H	0007339	biological_process	binding of sperm to zona pellucida
H	0016887	molecular_function	ATP hydrolysis activity
H	0032212	biological_process	positive regulation of telomere maintenance via telomerase
H	0043209	cellular_component	myelin sheath
H	0044183	molecular_function	protein folding chaperone
H	0044297	cellular_component	cell body
H	0050821	biological_process	protein stabilization
I	0002199	cellular_component	zona pellucida receptor complex
I	0005515	molecular_function	protein binding
I	0005654	cellular_component	nucleoplasm
I	0005737	cellular_component	cytoplasm
I	0005813	cellular_component	centrosome
I	0005829	cellular_component	cytosol
I	0005832	cellular_component	chaperonin-containing T-complex
I	0005874	cellular_component	microtubule
I	0006457	biological_process	protein folding
I	0007339	biological_process	binding of sperm to zona pellucida
I	0016887	molecular_function	ATP hydrolysis activity
I	0032212	biological_process	positive regulation of telomere maintenance via telomerase
I	0042470	cellular_component	melanosome
I	0044183	molecular_function	protein folding chaperone
I	0044297	cellular_component	cell body
I	0050821	biological_process	protein stabilization
I	0090666	biological_process	scaRNA localization to Cajal body
I	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	26
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGDGTTSVTVlAaellreaesl........IAKK

Chain	Residue	Details
G	VAL95-LYS120

---

site_id	PS00750
Number of Residues	13
Details	TCP1_1 Chaperonins TCP-1 signature 1. RTnLGPkGtmKML

Chain	Residue	Details
A	ARG35-LEU47
F	ARG49-MET61
C	LYS33-LEU45
G	LYS40-LEU52
B	ARG37-ILE49
E	ARG44-VAL56
H	ARG38-LEU50
I	ARG49-ILE61

---

site_id	PS00751
Number of Residues	17
Details	TCP1_2 Chaperonins TCP-1 signature 2. LTKDGNVLLheMqIqHP

Chain	Residue	Details
A	LEU56-PRO72
F	ILE70-GLN86
C	ILE54-PRO70
G	VAL63-PRO79
B	ILE58-PRO74
E	VAL65-PRO81
H	MET59-PRO75
I	ILE70-PRO86

---

site_id	PS00995
Number of Residues	9
Details	TCP1_3 Chaperonins TCP-1 signature 3. QDdiTGDGT

Chain	Residue	Details
A	GLN84-THR92
F	GLN98-THR106
C	GLN82-THR90
G	GLN91-THR99
B	GLN86-THR94
E	GLN93-THR101
H	GLN87-THR95
I	GLN98-THR106

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P17987","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P78371","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P49368","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P49368","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P50991","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P50991","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P48643","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P48643","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P40227","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q99832","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99832","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"Q99832","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI17
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI18
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O14737","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI19
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O14737","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---