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7M6J

Human Septin Hexameric Complex SEPT2G/SEPT6/SEPT7 by Single Particle Cryo-EM

Functional Information from GO Data
ChainGOidnamespacecontents
A0005525molecular_functionGTP binding
B0000166molecular_functionnucleotide binding
B0000281biological_processmitotic cytokinesis
B0000776cellular_componentkinetochore
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005819cellular_componentspindle
B0005940cellular_componentseptin ring
B0007010biological_processcytoskeleton organization
B0007283biological_processspermatogenesis
B0008021cellular_componentsynaptic vesicle
B0008104biological_processintracellular protein localization
B0015630cellular_componentmicrotubule cytoskeleton
B0030154biological_processcell differentiation
B0030496cellular_componentmidbody
B0031105cellular_componentseptin complex
B0031514cellular_componentmotile cilium
B0032153cellular_componentcell division site
B0032154cellular_componentcleavage furrow
B0032173cellular_componentseptin collar
B0043679cellular_componentaxon terminus
B0051301biological_processcell division
B0060090molecular_functionmolecular adaptor activity
B0061640biological_processcytoskeleton-dependent cytokinesis
B0097227cellular_componentsperm annulus
B0098793cellular_componentpresynapse
C0000166molecular_functionnucleotide binding
C0000776cellular_componentkinetochore
C0001725cellular_componentstress fiber
C0003924molecular_functionGTPase activity
C0005198molecular_functionstructural molecule activity
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005819cellular_componentspindle
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005929cellular_componentcilium
C0005930cellular_componentaxoneme
C0005940cellular_componentseptin ring
C0007010biological_processcytoskeleton organization
C0007283biological_processspermatogenesis
C0008104biological_processintracellular protein localization
C0015629cellular_componentactin cytoskeleton
C0015630cellular_componentmicrotubule cytoskeleton
C0016324cellular_componentapical plasma membrane
C0016476biological_processregulation of embryonic cell shape
C0030154biological_processcell differentiation
C0030496cellular_componentmidbody
C0031105cellular_componentseptin complex
C0031514cellular_componentmotile cilium
C0032153cellular_componentcell division site
C0032154cellular_componentcleavage furrow
C0042802molecular_functionidentical protein binding
C0045296molecular_functioncadherin binding
C0051301biological_processcell division
C0060090molecular_functionmolecular adaptor activity
C0060271biological_processcilium assembly
C0061640biological_processcytoskeleton-dependent cytokinesis
C0070062cellular_componentextracellular exosome
C0097227cellular_componentsperm annulus
C0097730cellular_componentnon-motile cilium
C1902857biological_processpositive regulation of non-motile cilium assembly
D0000166molecular_functionnucleotide binding
D0000776cellular_componentkinetochore
D0001725cellular_componentstress fiber
D0003924molecular_functionGTPase activity
D0005198molecular_functionstructural molecule activity
D0005515molecular_functionprotein binding
D0005525molecular_functionGTP binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005819cellular_componentspindle
D0005829cellular_componentcytosol
D0005856cellular_componentcytoskeleton
D0005929cellular_componentcilium
D0005930cellular_componentaxoneme
D0005940cellular_componentseptin ring
D0007010biological_processcytoskeleton organization
D0007283biological_processspermatogenesis
D0008104biological_processintracellular protein localization
D0015629cellular_componentactin cytoskeleton
D0015630cellular_componentmicrotubule cytoskeleton
D0016324cellular_componentapical plasma membrane
D0016476biological_processregulation of embryonic cell shape
D0030154biological_processcell differentiation
D0030496cellular_componentmidbody
D0031105cellular_componentseptin complex
D0031514cellular_componentmotile cilium
D0032153cellular_componentcell division site
D0032154cellular_componentcleavage furrow
D0042802molecular_functionidentical protein binding
D0045296molecular_functioncadherin binding
D0051301biological_processcell division
D0060090molecular_functionmolecular adaptor activity
D0060271biological_processcilium assembly
D0061640biological_processcytoskeleton-dependent cytokinesis
D0070062cellular_componentextracellular exosome
D0097227cellular_componentsperm annulus
D0097730cellular_componentnon-motile cilium
D1902857biological_processpositive regulation of non-motile cilium assembly
E0000166molecular_functionnucleotide binding
E0000281biological_processmitotic cytokinesis
E0000776cellular_componentkinetochore
E0003924molecular_functionGTPase activity
E0005515molecular_functionprotein binding
E0005525molecular_functionGTP binding
E0005737cellular_componentcytoplasm
E0005819cellular_componentspindle
E0005940cellular_componentseptin ring
E0007010biological_processcytoskeleton organization
E0007283biological_processspermatogenesis
E0008021cellular_componentsynaptic vesicle
E0008104biological_processintracellular protein localization
E0015630cellular_componentmicrotubule cytoskeleton
E0030154biological_processcell differentiation
E0030496cellular_componentmidbody
E0031105cellular_componentseptin complex
E0031514cellular_componentmotile cilium
E0032153cellular_componentcell division site
E0032154cellular_componentcleavage furrow
E0032173cellular_componentseptin collar
E0043679cellular_componentaxon terminus
E0051301biological_processcell division
E0060090molecular_functionmolecular adaptor activity
E0061640biological_processcytoskeleton-dependent cytokinesis
E0097227cellular_componentsperm annulus
E0098793cellular_componentpresynapse
F0005525molecular_functionGTP binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues42
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01056","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01056","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01056","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsRegion: {"description":"Important for dimerization"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues48
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues34
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Important for dimerization"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues532
DetailsDomain: {"description":"Septin-type G","evidences":[{"source":"PROSITE-ProRule","id":"PRU01056","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17637674","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O55131","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O55131","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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