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1S2H

The Mad2 spindle checkpoint protein possesses two distinct natively folded states

Functional Information from GO Data
ChainGOidnamespacecontents
A0000070biological_processmitotic sister chromatid segregation
A0000132biological_processestablishment of mitotic spindle orientation
A0000775cellular_componentchromosome, centromeric region
A0000776cellular_componentkinetochore
A0000922cellular_componentspindle pole
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0007094biological_processmitotic spindle assembly checkpoint signaling
A0033597cellular_componentmitotic checkpoint complex
A0042177biological_processnegative regulation of protein catabolic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043066biological_processnegative regulation of apoptotic process
A0044615cellular_componentnuclear pore nuclear basket
A0045930biological_processnegative regulation of mitotic cell cycle
A0048471cellular_componentperinuclear region of cytoplasm
A0051301biological_processcell division
A0051660biological_processestablishment of centrosome localization
A0072686cellular_componentmitotic spindle
A0090267biological_processpositive regulation of mitotic cell cycle spindle assembly checkpoint
A1904667biological_processnegative regulation of ubiquitin protein ligase activity
A1990728cellular_componentmitotic spindle assembly checkpoint MAD1-MAD2 complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.12
ChainResidueDetails
AALA2

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER6
ASER130
ASER185

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:12574116
ChainResidueDetails
ASER170
ASER178

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:12574116, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER195

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PDB entries from 2024-07-17

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