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3UIG

crystal structure of human Survivin in complex with T3 phosphorylated H3(1-15) peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000228cellular_componentnuclear chromosome
A0000278biological_processmitotic cell cycle
A0000281biological_processmitotic cytokinesis
A0000775cellular_componentchromosome, centromeric region
A0000776cellular_componentkinetochore
A0004869molecular_functioncysteine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0005737cellular_componentcytoplasm
A0005819cellular_componentspindle
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0007049biological_processcell cycle
A0007059biological_processchromosome segregation
A0007605biological_processsensory perception of sound
A0008017molecular_functionmicrotubule binding
A0008284biological_processpositive regulation of cell population proliferation
A0015630cellular_componentmicrotubule cytoskeleton
A0019899molecular_functionenzyme binding
A0030414molecular_functionpeptidase inhibitor activity
A0030496cellular_componentmidbody
A0031267molecular_functionsmall GTPase binding
A0031503biological_processprotein-containing complex localization
A0032133cellular_componentchromosome passenger complex
A0042802molecular_functionidentical protein binding
A0042981biological_processregulation of apoptotic process
A0043066biological_processnegative regulation of apoptotic process
A0045892biological_processnegative regulation of DNA-templated transcription
A0046872molecular_functionmetal ion binding
A0051087molecular_functionprotein-folding chaperone binding
A0051256biological_processmitotic spindle midzone assembly
A0051301biological_processcell division
A0090267biological_processpositive regulation of mitotic cell cycle spindle assembly checkpoint
A0090307biological_processmitotic spindle assembly
A1901970biological_processpositive regulation of mitotic sister chromatid separation
A1902425biological_processpositive regulation of attachment of mitotic spindle microtubules to kinetochore
A1903490biological_processpositive regulation of mitotic cytokinesis
A1990713cellular_componentsurvivin complex
B0000228cellular_componentnuclear chromosome
B0000278biological_processmitotic cell cycle
B0000281biological_processmitotic cytokinesis
B0000775cellular_componentchromosome, centromeric region
B0000776cellular_componentkinetochore
B0004869molecular_functioncysteine-type endopeptidase inhibitor activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0005737cellular_componentcytoplasm
B0005819cellular_componentspindle
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0006468biological_processprotein phosphorylation
B0006915biological_processapoptotic process
B0007049biological_processcell cycle
B0007059biological_processchromosome segregation
B0007605biological_processsensory perception of sound
B0008017molecular_functionmicrotubule binding
B0008284biological_processpositive regulation of cell population proliferation
B0015630cellular_componentmicrotubule cytoskeleton
B0019899molecular_functionenzyme binding
B0030414molecular_functionpeptidase inhibitor activity
B0030496cellular_componentmidbody
B0031267molecular_functionsmall GTPase binding
B0031503biological_processprotein-containing complex localization
B0032133cellular_componentchromosome passenger complex
B0042802molecular_functionidentical protein binding
B0042981biological_processregulation of apoptotic process
B0043066biological_processnegative regulation of apoptotic process
B0045892biological_processnegative regulation of DNA-templated transcription
B0046872molecular_functionmetal ion binding
B0051087molecular_functionprotein-folding chaperone binding
B0051256biological_processmitotic spindle midzone assembly
B0051301biological_processcell division
B0090267biological_processpositive regulation of mitotic cell cycle spindle assembly checkpoint
B0090307biological_processmitotic spindle assembly
B1901970biological_processpositive regulation of mitotic sister chromatid separation
B1902425biological_processpositive regulation of attachment of mitotic spindle microtubules to kinetochore
B1903490biological_processpositive regulation of mitotic cytokinesis
B1990713cellular_componentsurvivin complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 341
ChainResidue
ACYS57
ACYS60
AHIS77
ACYS84

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 341
ChainResidue
BCYS57
BCYS60
BHIS77
BCYS84

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Citrulline; alternate => ECO:0000269|PubMed:16567635
ChainResidueDetails
PARG2
QARG2
AHIS77
ACYS84
BCYS57
BCYS60
BHIS77
BCYS84

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
ChainResidueDetails
PTPO3
QTPO3

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
ChainResidueDetails
QLYS4
PLYS4

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
ChainResidueDetails
PGLN5
QGLN5
ALYS110
ALYS112
ALYS115
ALYS121
ALYS129
BLYS23
BLYS90
BLYS110
BLYS112
BLYS115
BLYS121
BLYS129

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
ChainResidueDetails
PTHR6
QTHR6

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
ChainResidueDetails
PARG8
QARG8

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
ChainResidueDetails
QLYS9
PLYS9

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588
ChainResidueDetails
PSER10
QSER10

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803
ChainResidueDetails
PTHR11
QTHR11

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
PLYS14
QLYS14

218500

PDB entries from 2024-04-17

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