O42649 · SMC3_SCHPO
- ProteinStructural maintenance of chromosomes protein 3
- Genepsm3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1194 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | cohesin complex | |
Cellular Component | condensed chromosome, centromeric region | |
Cellular Component | cytosol | |
Cellular Component | meiotic cohesin complex | |
Cellular Component | mitotic cohesin complex | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | DNA binding | |
Biological Process | cell division | |
Biological Process | chromatin looping | |
Biological Process | mitotic sister chromatid cohesion |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameStructural maintenance of chromosomes protein 3
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionO42649
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associates with chromatin. Before prophase it is scattered along chromosome arms. At anaphase, the rad21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000119014 | 1-1194 | Structural maintenance of chromosomes protein 3 | |||
Sequence: MYITKIVIQGFKSYKDYTVIEPLSPHHNVIVGRNGSGKSNFFAAIRFVLSDAYTHLSREERQALLHEGPGATVMSAYVEVTFANADNRFPTGKSEVVLRRTIGLKKDEYSLDKKTVSKTEVINLLESAGFSRSNPYYIVPQGRVTSLTNAKDSERLELLKEVAGTQIYENRRAESNKIMDETIQKSEKIDELLQYIEERLRELEEEKNDLAVYHKKDNERRCLEYAIYSREHDEINSVLDALEQDRIAALERNDDDSGAFIQREERIERIKAEITELNHSLELLRVEKQQNDEDYTNIMKSKVALELQSSQLSRQIEFSKKDESSKLNILSELESKISEKENELSEILPKYNAIVSEADDLNKRIMLLKNQKQSLLDKQSRTSQFTTKKERDEWIRNQLLQINRNINSTKENSDYLKTEYDEMENELKAKLSRKKEIEISLESQGDRMSQLLANITSINERKENLTDKRKSLWREEAKLKSSIENVKDDLSRSEKALGTTMDRNTSNGIRAVKDIAERLKLEGYYGPLCELFKVDNRFKVAVEATAGNSLFHIVVDNDETATQILDVIYKENAGRVTFMPLNKLRPKAVTYPDASDALPLIQYLEFDPKFDAAIKQVFSKTIVCPSIETASQYARSHQLNGITLSGDRSDKKGALTAGYRDYRNSRLDAIKNVKTYQIKFSDLQESLEKCRSEIESFDQKITACLDDLQKAQLSLKQFERDHIPLKDELVTITGETTDLQESMHHKSRMLELVVLELHTLEQQANDLKSELSSEMDELDPKDVEALKSLSGQIENLSHEFDAIIKERAHIEARKTALEYELNTNLYLRRNPLKAEIGSDNRIDESELNSVKRSLLKYENKLQIIKSSSSGLEEQMQRINSEISDKRNELESLEELQHEVATRIEQDAKINERNAAKRSLLLARKKECNEKIKSLGVLPEEAFIKYVSTSSNAIVKKLHKINEALKDYGSVNKKAYEQFNNFTKQRDSLLARREELRRSQESISELTTVLDQRKDEAIERTFKQVAKSFSEIFVKLVPAGRGELVMNRRSELSQSIEQDISMDIDTPSQKSSIDNYTGISIRVSFNSKDDEQLNINQLSGGQKSLCALTLIFAIQRCDPAPFNILDECDANLDAQYRSAIAAMVKEMSKTSQFICTTFRPEMVKVADNFYGVMFNHKVSTVESISKEEAMAFVEG | ||||||
Modified residue | 105 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 106 | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Acetylation at Lys-105 and Lys-106 by ECO1 is important for genome stability and S phase sister chromatid cohesion.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Cohesin complexes are composed of the psm1/smc1 and psm3/smc3 heterodimer attached via their SMC hinge domain, rad21/scc1 which link them, and psc3/scc3, which interacts with rad21.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O42649 | mis4 Q09725 | 3 | EBI-1151879, EBI-16083239 | |
BINARY | O42649 | psm1 O94383 | 3 | EBI-1151879, EBI-1151900 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 176-497 | |||||
Sequence: NKIMDETIQKSEKIDELLQYIEERLRELEEEKNDLAVYHKKDNERRCLEYAIYSREHDEINSVLDALEQDRIAALERNDDDSGAFIQREERIERIKAEITELNHSLELLRVEKQQNDEDYTNIMKSKVALELQSSQLSRQIEFSKKDESSKLNILSELESKISEKENELSEILPKYNAIVSEADDLNKRIMLLKNQKQSLLDKQSRTSQFTTKKERDEWIRNQLLQINRNINSTKENSDYLKTEYDEMENELKAKLSRKKEIEISLESQGDRMSQLLANITSINERKENLTDKRKSLWREEAKLKSSIENVKDDLSRSEKAL | ||||||
Domain | 522-634 | SMC hinge | ||||
Sequence: EGYYGPLCELFKVDNRFKVAVEATAGNSLFHIVVDNDETATQILDVIYKENAGRVTFMPLNKLRPKAVTYPDASDALPLIQYLEFDPKFDAAIKQVFSKTIVCPSIETASQYA | ||||||
Coiled coil | 668-908 | |||||
Sequence: DAIKNVKTYQIKFSDLQESLEKCRSEIESFDQKITACLDDLQKAQLSLKQFERDHIPLKDELVTITGETTDLQESMHHKSRMLELVVLELHTLEQQANDLKSELSSEMDELDPKDVEALKSLSGQIENLSHEFDAIIKERAHIEARKTALEYELNTNLYLRRNPLKAEIGSDNRIDESELNSVKRSLLKYENKLQIIKSSSSGLEEQMQRINSEISDKRNELESLEELQHEVATRIEQDAK | ||||||
Coiled coil | 970-1006 | |||||
Sequence: VNKKAYEQFNNFTKQRDSLLARREELRRSQESISELT |
Domain
The flexible SMC hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of psm1, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable rad21 protein, forming a ring structure (By similarity).
Sequence similarities
Belongs to the SMC family. SMC3 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,194
- Mass (Da)136,850
- Last updated1998-06-01 v1
- ChecksumFD4D1E81A9E2E423
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU329670 EMBL· GenBank· DDBJ | CAA15722.1 EMBL· GenBank· DDBJ | Genomic DNA |