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6EPC

Ground state 26S proteasome (GS2)

Functional Information from GO Data
ChainGOidnamespacecontents
10000502cellular_componentproteasome complex
10004175molecular_functionendopeptidase activity
10004298molecular_functionthreonine-type endopeptidase activity
10005634cellular_componentnucleus
10005654cellular_componentnucleoplasm
10005737cellular_componentcytoplasm
10005739cellular_componentmitochondrion
10005829cellular_componentcytosol
10005839cellular_componentproteasome core complex
10006508biological_processproteolysis
10008233molecular_functionpeptidase activity
10016787molecular_functionhydrolase activity
10019774cellular_componentproteasome core complex, beta-subunit complex
10043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
10051603biological_processproteolysis involved in protein catabolic process
20000502cellular_componentproteasome complex
20004175molecular_functionendopeptidase activity
20004298molecular_functionthreonine-type endopeptidase activity
20005634cellular_componentnucleus
20005654cellular_componentnucleoplasm
20005737cellular_componentcytoplasm
20005829cellular_componentcytosol
20005839cellular_componentproteasome core complex
20005929cellular_componentcilium
20006508biological_processproteolysis
20008233molecular_functionpeptidase activity
20016604cellular_componentnuclear body
20016787molecular_functionhydrolase activity
20019774cellular_componentproteasome core complex, beta-subunit complex
20043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
20051603biological_processproteolysis involved in protein catabolic process
30000502cellular_componentproteasome complex
30005634cellular_componentnucleus
30005737cellular_componentcytoplasm
30005829cellular_componentcytosol
30005839cellular_componentproteasome core complex
30019774cellular_componentproteasome core complex, beta-subunit complex
30043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
30051603biological_processproteolysis involved in protein catabolic process
40000502cellular_componentproteasome complex
40005634cellular_componentnucleus
40005654cellular_componentnucleoplasm
40005737cellular_componentcytoplasm
40005829cellular_componentcytosol
40005839cellular_componentproteasome core complex
40010498biological_processproteasomal protein catabolic process
40019774cellular_componentproteasome core complex, beta-subunit complex
40043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
40051603biological_processproteolysis involved in protein catabolic process
50000502cellular_componentproteasome complex
50004175molecular_functionendopeptidase activity
50004298molecular_functionthreonine-type endopeptidase activity
50005634cellular_componentnucleus
50005654cellular_componentnucleoplasm
50005737cellular_componentcytoplasm
50005813cellular_componentcentrosome
50005829cellular_componentcytosol
50005839cellular_componentproteasome core complex
50006508biological_processproteolysis
50006979biological_processresponse to oxidative stress
50008233molecular_functionpeptidase activity
50016787molecular_functionhydrolase activity
50019774cellular_componentproteasome core complex, beta-subunit complex
50043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
50051603biological_processproteolysis involved in protein catabolic process
60000502cellular_componentproteasome complex
60005634cellular_componentnucleus
60005654cellular_componentnucleoplasm
60005737cellular_componentcytoplasm
60005839cellular_componentproteasome core complex
60019774cellular_componentproteasome core complex, beta-subunit complex
60051603biological_processproteolysis involved in protein catabolic process
70000502cellular_componentproteasome complex
70001530molecular_functionlipopolysaccharide binding
70002862biological_processnegative regulation of inflammatory response to antigenic stimulus
70005634cellular_componentnucleus
70005654cellular_componentnucleoplasm
70005737cellular_componentcytoplasm
70005739cellular_componentmitochondrion
70005829cellular_componentcytosol
70005839cellular_componentproteasome core complex
70019774cellular_componentproteasome core complex, beta-subunit complex
70036064cellular_componentciliary basal body
70043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
70051603biological_processproteolysis involved in protein catabolic process
A0000502cellular_componentproteasome complex
A0000932cellular_componentP-body
A0003723molecular_functionRNA binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005839cellular_componentproteasome core complex
A0005840cellular_componentribosome
A0005929cellular_componentcilium
A0006511biological_processubiquitin-dependent protein catabolic process
A0016363cellular_componentnuclear matrix
A0019773cellular_componentproteasome core complex, alpha-subunit complex
A0030016cellular_componentmyofibril
A0030017cellular_componentsarcomere
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0050727biological_processregulation of inflammatory response
A0051059molecular_functionNF-kappaB binding
A0051603biological_processproteolysis involved in protein catabolic process
B0000502cellular_componentproteasome complex
B0000932cellular_componentP-body
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005839cellular_componentproteasome core complex
B0006511biological_processubiquitin-dependent protein catabolic process
B0009615biological_processresponse to virus
B0019773cellular_componentproteasome core complex, alpha-subunit complex
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0051603biological_processproteolysis involved in protein catabolic process
C0000502cellular_componentproteasome complex
C0000932cellular_componentP-body
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005839cellular_componentproteasome core complex
C0006511biological_processubiquitin-dependent protein catabolic process
C0019773cellular_componentproteasome core complex, alpha-subunit complex
C0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
C0051603biological_processproteolysis involved in protein catabolic process
D0000502cellular_componentproteasome complex
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005839cellular_componentproteasome core complex
D0006511biological_processubiquitin-dependent protein catabolic process
D0019773cellular_componentproteasome core complex, alpha-subunit complex
D0042802molecular_functionidentical protein binding
D0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
D0051603biological_processproteolysis involved in protein catabolic process
E0000502cellular_componentproteasome complex
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005839cellular_componentproteasome core complex
E0006511biological_processubiquitin-dependent protein catabolic process
E0019773cellular_componentproteasome core complex, alpha-subunit complex
E0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
E0051603biological_processproteolysis involved in protein catabolic process
F0000502cellular_componentproteasome complex
F0001530molecular_functionlipopolysaccharide binding
F0002376biological_processimmune system process
F0002862biological_processnegative regulation of inflammatory response to antigenic stimulus
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005737cellular_componentcytoplasm
F0005813cellular_componentcentrosome
F0005829cellular_componentcytosol
F0005839cellular_componentproteasome core complex
F0006511biological_processubiquitin-dependent protein catabolic process
F0019773cellular_componentproteasome core complex, alpha-subunit complex
F0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
F0051603biological_processproteolysis involved in protein catabolic process
G0000502cellular_componentproteasome complex
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0005839cellular_componentproteasome core complex
G0006511biological_processubiquitin-dependent protein catabolic process
G0019773cellular_componentproteasome core complex, alpha-subunit complex
G0031625molecular_functionubiquitin protein ligase binding
G0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
G0051603biological_processproteolysis involved in protein catabolic process
H0000166molecular_functionnucleotide binding
H0000502cellular_componentproteasome complex
H0000932cellular_componentP-body
H0005524molecular_functionATP binding
H0005737cellular_componentcytoplasm
H0005829cellular_componentcytosol
H0006511biological_processubiquitin-dependent protein catabolic process
H0008540cellular_componentproteasome regulatory particle, base subcomplex
H0016887molecular_functionATP hydrolysis activity
H0017025molecular_functionTBP-class protein binding
H0022624cellular_componentproteasome accessory complex
H0036402molecular_functionproteasome-activating activity
H0036464cellular_componentcytoplasmic ribonucleoprotein granule
H0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
H0140296molecular_functiongeneral transcription initiation factor binding
I0000166molecular_functionnucleotide binding
I0000502cellular_componentproteasome complex
I0005524molecular_functionATP binding
I0005634cellular_componentnucleus
I0005654cellular_componentnucleoplasm
I0005737cellular_componentcytoplasm
I0005829cellular_componentcytosol
I0005838cellular_componentproteasome regulatory particle
I0008150biological_processbiological_process
I0008540cellular_componentproteasome regulatory particle, base subcomplex
I0016020cellular_componentmembrane
I0016887molecular_functionATP hydrolysis activity
I0017025molecular_functionTBP-class protein binding
I0022624cellular_componentproteasome accessory complex
I0036402molecular_functionproteasome-activating activity
I0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
J0000166molecular_functionnucleotide binding
J0000502cellular_componentproteasome complex
J0005102molecular_functionsignaling receptor binding
J0005524molecular_functionATP binding
J0005634cellular_componentnucleus
J0005737cellular_componentcytoplasm
J0005838cellular_componentproteasome regulatory particle
J0006357biological_processregulation of transcription by RNA polymerase II
J0008540cellular_componentproteasome regulatory particle, base subcomplex
J0016234cellular_componentinclusion body
J0016887molecular_functionATP hydrolysis activity
J0017025molecular_functionTBP-class protein binding
J0022624cellular_componentproteasome accessory complex
J0031410cellular_componentcytoplasmic vesicle
J0031531molecular_functionthyrotropin-releasing hormone receptor binding
J0031595cellular_componentnuclear proteasome complex
J0031597cellular_componentcytosolic proteasome complex
J0036402molecular_functionproteasome-activating activity
J0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
J0045892biological_processnegative regulation of DNA-templated transcription
J0090261biological_processpositive regulation of inclusion body assembly
J0140296molecular_functiongeneral transcription initiation factor binding
J0140297molecular_functionDNA-binding transcription factor binding
K0000166molecular_functionnucleotide binding
K0000502cellular_componentproteasome complex
K0001824biological_processblastocyst development
K0005524molecular_functionATP binding
K0005634cellular_componentnucleus
K0005654cellular_componentnucleoplasm
K0005737cellular_componentcytoplasm
K0005829cellular_componentcytosol
K0008540cellular_componentproteasome regulatory particle, base subcomplex
K0016234cellular_componentinclusion body
K0016887molecular_functionATP hydrolysis activity
K0022624cellular_componentproteasome accessory complex
K0031597cellular_componentcytosolic proteasome complex
K0036064cellular_componentciliary basal body
K0036402molecular_functionproteasome-activating activity
K0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
L0000166molecular_functionnucleotide binding
L0000502cellular_componentproteasome complex
L0005524molecular_functionATP binding
L0005634cellular_componentnucleus
L0005737cellular_componentcytoplasm
L0016234cellular_componentinclusion body
L0016887molecular_functionATP hydrolysis activity
L0022624cellular_componentproteasome accessory complex
L0031597cellular_componentcytosolic proteasome complex
L0042802molecular_functionidentical protein binding
L0090261biological_processpositive regulation of inclusion body assembly
M0000166molecular_functionnucleotide binding
M0000502cellular_componentproteasome complex
M0000932cellular_componentP-body
M0001824biological_processblastocyst development
M0005515molecular_functionprotein binding
M0005524molecular_functionATP binding
M0005634cellular_componentnucleus
M0005737cellular_componentcytoplasm
M0008540cellular_componentproteasome regulatory particle, base subcomplex
M0016887molecular_functionATP hydrolysis activity
M0022624cellular_componentproteasome accessory complex
M0036402molecular_functionproteasome-activating activity
M0042802molecular_functionidentical protein binding
M0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
M0043921biological_processhost-mediated perturbation of viral transcription
M0045944biological_processpositive regulation of transcription by RNA polymerase II
M0048471cellular_componentperinuclear region of cytoplasm
N0000502cellular_componentproteasome complex
N0005634cellular_componentnucleus
N0008540cellular_componentproteasome regulatory particle, base subcomplex
N0022624cellular_componentproteasome accessory complex
N0030234molecular_functionenzyme regulator activity
N0031625molecular_functionubiquitin protein ligase binding
N0034515cellular_componentproteasome storage granule
N0042176biological_processregulation of protein catabolic process
N0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
O0000502cellular_componentproteasome complex
O0005198molecular_functionstructural molecule activity
O0005634cellular_componentnucleus
O0005829cellular_componentcytosol
O0005838cellular_componentproteasome regulatory particle
O0006511biological_processubiquitin-dependent protein catabolic process
O0007127biological_processmeiosis I
O0008541cellular_componentproteasome regulatory particle, lid subcomplex
O0022624cellular_componentproteasome accessory complex
P0000502cellular_componentproteasome complex
P0005737cellular_componentcytoplasm
P0005838cellular_componentproteasome regulatory particle
P0008541cellular_componentproteasome regulatory particle, lid subcomplex
P0022624cellular_componentproteasome accessory complex
Q0000502cellular_componentproteasome complex
Q0005198molecular_functionstructural molecule activity
Q0005634cellular_componentnucleus
Q0005829cellular_componentcytosol
Q0005838cellular_componentproteasome regulatory particle
Q0006511biological_processubiquitin-dependent protein catabolic process
Q0008541cellular_componentproteasome regulatory particle, lid subcomplex
Q0022624cellular_componentproteasome accessory complex
Q0043248biological_processproteasome assembly
Q0048863biological_processstem cell differentiation
R0000502cellular_componentproteasome complex
R0022624cellular_componentproteasome accessory complex
S0000502cellular_componentproteasome complex
S0005654cellular_componentnucleoplasm
S0005829cellular_componentcytosol
S0005838cellular_componentproteasome regulatory particle
S0022624cellular_componentproteasome accessory complex
S0030234molecular_functionenzyme regulator activity
S0042176biological_processregulation of protein catabolic process
T0000502cellular_componentproteasome complex
T0005634cellular_componentnucleus
T0005838cellular_componentproteasome regulatory particle
T0006508biological_processproteolysis
T0008541cellular_componentproteasome regulatory particle, lid subcomplex
T0022624cellular_componentproteasome accessory complex
T0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
U0005838cellular_componentproteasome regulatory particle
U0008233molecular_functionpeptidase activity
U0008237molecular_functionmetallopeptidase activity
V0008233molecular_functionpeptidase activity
V0008237molecular_functionmetallopeptidase activity
W0000502cellular_componentproteasome complex
Y0000502cellular_componentproteasome complex
Y0000724biological_processdouble-strand break repair via homologous recombination
Y0005634cellular_componentnucleus
Y0006406biological_processmRNA export from nucleus
Y0008541cellular_componentproteasome regulatory particle, lid subcomplex
Y0032039cellular_componentintegrator complex
Y0032991cellular_componentprotein-containing complex
Y0043248biological_processproteasome assembly
Z0000502cellular_componentproteasome complex
Z0005634cellular_componentnucleus
Z0005838cellular_componentproteasome regulatory particle
Z0008540cellular_componentproteasome regulatory particle, base subcomplex
Z0022624cellular_componentproteasome accessory complex
Z0030234molecular_functionenzyme regulator activity
Z0034515cellular_componentproteasome storage granule
Z0042176biological_processregulation of protein catabolic process
Z0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
Functional Information from PROSITE/UniProt
site_idPS00012
Number of Residues16
DetailsPHOSPHOPANTETHEINE Phosphopantetheine attachment site. TTGVSSSGPAATSGGI
ChainResidueDetails
TTHR75-ILE90

site_idPS00388
Number of Residues23
DetailsPROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdrgvNtFSPeGRlfQVEYAieG
ChainResidueDetails
ETYR8-GLY30
APHE9-ALA31
CTYR5-ALA27
DTYR3-ALA25
BTYR6-ALA28
GTYR8-ALA30
FTYR6-ALA28

site_idPS00674
Number of Residues19
DetailsAAA AAA-protein family signature. VkVImATNradtLDpALl.R
ChainResidueDetails
KVAL305-ARG323
HILE315-ARG333
JILE289-ARG307
IVAL325-ARG343
MVAL329-ARG347
LVAL287-ARG305

site_idPS00854
Number of Residues48
DetailsPROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFqhGVIVAADsratagpyiasqtvk.KvieinpyllgtmaGgaAD
ChainResidueDetails
5LEU63-ASP110
1MET37-ASP84
CLEU35-ASP82
3MET12-ASP59
2ALA47-ASP94
6LEU40-ASP87
4ILE5-ASP52
7LEU56-ASP103

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P60900","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P60900","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9QUM9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"2335242","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P49722","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P25787","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P25787","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P25787","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"8794741","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P25789","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P25789","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O14818","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O14818","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues5
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P28066","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P28066","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; alternate","evidences":[{"source":"UniProtKB","id":"P25786","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P25786","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine; alternate","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P25786","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"2335242","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P25788","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P28072","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P28072","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2007","submissionDatabase":"UniProtKB","authors":["Lubec G.","Chen W.-Q."]}}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P49720","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P49721","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P28074","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI32
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P20618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O09061","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI34
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P20618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI35
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P28070","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI39
Number of Residues66
DetailsRepeat: {"description":"PC 1"}
ChainResidueDetails

site_idSWS_FT_FI40
Number of Residues69
DetailsRepeat: {"description":"PC 2"}
ChainResidueDetails

site_idSWS_FT_FI41
Number of Residues68
DetailsRepeat: {"description":"PC 3"}
ChainResidueDetails

site_idSWS_FT_FI42
Number of Residues68
DetailsRepeat: {"description":"PC 4"}
ChainResidueDetails

site_idSWS_FT_FI43
Number of Residues62
DetailsRepeat: {"description":"PC 5"}
ChainResidueDetails

site_idSWS_FT_FI44
Number of Residues66
DetailsRepeat: {"description":"PC 6"}
ChainResidueDetails

site_idSWS_FT_FI45
Number of Residues47
DetailsRepeat: {"description":"PC 7"}
ChainResidueDetails

site_idSWS_FT_FI46
Number of Residues157
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI47
Number of Residues10
DetailsCompositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI48
Number of Residues96
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI49
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"Q8VDM4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI50
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q8VDM4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI51
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q13200","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI52
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q13200","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI53
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8VDM4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI54
Number of Residues34
DetailsRepeat: {"description":"PC 8"}
ChainResidueDetails

site_idSWS_FT_FI55
Number of Residues40
DetailsRepeat: {"description":"PC 9"}
ChainResidueDetails

site_idSWS_FT_FI56
Number of Residues32
DetailsRepeat: {"description":"PC 10"}
ChainResidueDetails

site_idSWS_FT_FI57
Number of Residues17
DetailsCompositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI58
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"Q99460","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI59
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI60
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q3TXS7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI61
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q99460","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI62
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q99460","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI63
Number of Residues335
DetailsDomain: {"description":"PCI","evidences":[{"source":"PROSITE-ProRule","id":"PRU01185","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI64
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"O00231","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI65
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O00231","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI66
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"O00231","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI68
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9UNM6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI69
Number of Residues35
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI70
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P35998","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI71
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI72
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI73
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI74
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P62191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI75
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P43686","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI76
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P43686","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI78
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P17980","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI79
Number of Residues220
DetailsRegion: {"description":"May mediate interaction with PRPF9","evidences":[{"source":"UniProtKB","id":"P62196","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI80
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P62195","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI81
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62195","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI82
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62195","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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