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8RUP

Chromosome Passenger Complex (CPC) localization module in complex with H3.T3p-nucleosome

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0030527molecular_functionstructural constituent of chromatin
A0046982molecular_functionprotein heterodimerization activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0006334biological_processnucleosome assembly
B0030527molecular_functionstructural constituent of chromatin
B0046982molecular_functionprotein heterodimerization activity
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0030527molecular_functionstructural constituent of chromatin
C0031507biological_processheterochromatin formation
C0046982molecular_functionprotein heterodimerization activity
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
D0030527molecular_functionstructural constituent of chromatin
D0046982molecular_functionprotein heterodimerization activity
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005634cellular_componentnucleus
E0005694cellular_componentchromosome
E0030527molecular_functionstructural constituent of chromatin
E0046982molecular_functionprotein heterodimerization activity
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0006334biological_processnucleosome assembly
F0030527molecular_functionstructural constituent of chromatin
F0046982molecular_functionprotein heterodimerization activity
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0030527molecular_functionstructural constituent of chromatin
G0031507biological_processheterochromatin formation
G0046982molecular_functionprotein heterodimerization activity
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005694cellular_componentchromosome
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
K0000228cellular_componentnuclear chromosome
K0000278biological_processmitotic cell cycle
K0000281biological_processmitotic cytokinesis
K0000775cellular_componentchromosome, centromeric region
K0000776cellular_componentkinetochore
K0004869molecular_functioncysteine-type endopeptidase inhibitor activity
K0005515molecular_functionprotein binding
K0005634cellular_componentnucleus
K0005654cellular_componentnucleoplasm
K0005694cellular_componentchromosome
K0005737cellular_componentcytoplasm
K0005819cellular_componentspindle
K0005829cellular_componentcytosol
K0005856cellular_componentcytoskeleton
K0005874cellular_componentmicrotubule
K0006915biological_processapoptotic process
K0007052biological_processmitotic spindle organization
K0007059biological_processchromosome segregation
K0007605biological_processsensory perception of sound
K0008017molecular_functionmicrotubule binding
K0008284biological_processpositive regulation of cell population proliferation
K0015630cellular_componentmicrotubule cytoskeleton
K0019899molecular_functionenzyme binding
K0030414molecular_functionpeptidase inhibitor activity
K0030496cellular_componentmidbody
K0031267molecular_functionsmall GTPase binding
K0031503biological_processprotein-containing complex localization
K0032133cellular_componentchromosome passenger complex
K0042802molecular_functionidentical protein binding
K0043066biological_processnegative regulation of apoptotic process
K0045892biological_processnegative regulation of DNA-templated transcription
K0046872molecular_functionmetal ion binding
K0051087molecular_functionprotein-folding chaperone binding
K0051233cellular_componentspindle midzone
K0051256biological_processmitotic spindle midzone assembly
K0051301biological_processcell division
K0090267biological_processpositive regulation of mitotic cell cycle spindle assembly checkpoint
K0090307biological_processmitotic spindle assembly
K1901970biological_processpositive regulation of mitotic sister chromatid separation
K1902425biological_processpositive regulation of attachment of mitotic spindle microtubules to kinetochore
K1903490biological_processpositive regulation of mitotic cytokinesis
K1990713cellular_componentsurvivin complex
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ELYS14-LEU20
ALYS14-LEU20

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG92-GLY114

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
EPRO66-ILE74
APRO66-ILE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues4
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues2
DetailsModified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P0C1H4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues70
DetailsRepeat: {"description":"BIR"}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17956729","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QFA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues1
DetailsSite: {"description":"Interaction with FBXL7","evidences":[{"source":"PubMed","id":"25778398","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by AURKC","evidences":[{"source":"PubMed","id":"27332895","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI32
Number of Residues7
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"20826784","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CDK1 and CDK15","evidences":[{"source":"PubMed","id":"11069302","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24866247","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI34
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CK2; in vitro","evidences":[{"source":"PubMed","id":"21252625","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI35
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by AURKB","evidences":[{"source":"PubMed","id":"14610074","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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