P40541 · SCC3_YEAST
- ProteinCohesin subunit SCC3
- GeneIRR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1150 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of cohesin complex, a complex 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 MCD1/SCC1 subunit of the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.
Miscellaneous
Present with 4090 molecules/cell in log phase SD medium.
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 | chromatin | |
Cellular Component | chromosome, centromeric region | |
Cellular Component | cohesin complex | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | meiotic cohesin complex | |
Cellular Component | mitotic cohesin complex | |
Cellular Component | nucleus | |
Molecular Function | chromatin binding | |
Biological Process | cell division | |
Biological Process | chromosome segregation | |
Biological Process | establishment of meiotic sister chromatid cohesion | |
Biological Process | establishment of mitotic sister chromatid cohesion | |
Biological Process | mitotic sister chromatid cohesion | |
Biological Process | protein acetylation | |
Biological Process | sister chromatid cohesion |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCohesin subunit SCC3
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP40541
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin except at centromeres, where cohesin complexes remain. At anaphase, the MCD1 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_0000120191 | 1-1150 | Cohesin subunit SCC3 | |||
Sequence: MTAVRRSTRIRTKSQVIEEDYDDEQNTSAQHVESDKITAKTQHEEEEEQDTGESEESSSEDDYEDQDDDDYVDTATAKRKSRKRKPKSASNTSSKRQKKKPTSAQKSAVSHAPAYHRSKKDQDQYLEIAKDFQPTELFDILSTSEDVSIEELLREWLETYSENRDKFLQEFINLLLNCCGSVARVEDHDVHSNESSNETIGEIQLLFQRQKLHEFYLLISKENKKRKNFKMGPLYQNFAEFMTKLLEVANDLQLLYVESDEDDTQIVTGNLVLDLLTWLSSFSVCKIRCFRYISTLTLYLFQDYLTQQAVNLEKNYLAKLSKQLSLEEKKKRPNNKTLEKLESTIAETQGSKVVIDSIIDNIVKLCFVHRYKDVSDLIRSESMLHLSIWIKNYPEYFLKVTFLKYFGWLLSDNSVSVRLQVTKILPHLIIQNHNSKSTDNSAIRQVFERFKTKILEVAIRDVNLDVRIHSIQVLTEASSLGYLDDSEILIISSLMFDEEFDPFKTSSFNKRSKFLSTVAKFLARVIKEKFDEFIKTHEDLPKEVDGLEVGPVVQVGIFIKILNDSLIYHLKDCAEVDSRTKIRMLTQAAEFLSPYISTHLKTICNLLISDTESNELIQKLQNSANNNSDDEDVDDEELDITPLFPIDRNSTILYLNVFHGLCAGANNPKIQTKDSVKEIVLPLFYDLLNAASIESADILCPLLESFITFSLDDWISIGYETELKKITDKTIKAFMDSTIGNSKVDMKYDIFAKFIHHIHHFEKKELQEKFLNQIATLKIHLKKFLQEKMDPNNSRDDYKDLTCSLYELYINKLTILGRDYPIEVDEELLQLFLNNFVSRIPIMFQDFDDSTAQEINFKMLVLLATWNLEKWREIIEKVRDYENSISKDLRSVWKPIAAIIGRLNTLVISLAATNETFENINSLFYLKWSACTSLMDIIVAIKIFELKLPADATTWRYSMSEQFPFYLHDNASKVLLKIFLYLESLFAKQVDVQLERVADEDANLNDLPETGFFENIETEFLLFTVKLKGLMKLNILDERFASRVALNKEKLGPLFKKIVDDTIMENPEPNKKNIQKAKSNQTQREKAPLQPNSERETDHANTENNDPDIPMTIDLEPIEESSQNNSELAPIEEHPTVVDAIDNSDEITQD | ||||||
Modified residue | 28 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 628 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Acetylated by ECO1.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts directly with MCD1 in cohesin complex. Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1 which link them, and IRR1/SCC3, which interacts with MCD1. The cohesin complex also interacts with SCC2, which is required for its association with chromosomes. Interacts with LIN1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P40541 | MCD1 Q12158 | 8 | EBI-16667, EBI-16655 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-122 | Disordered | ||||
Sequence: MTAVRRSTRIRTKSQVIEEDYDDEQNTSAQHVESDKITAKTQHEEEEEQDTGESEESSSEDDYEDQDDDDYVDTATAKRKSRKRKPKSASNTSSKRQKKKPTSAQKSAVSHAPAYHRSKKDQ | ||||||
Compositional bias | 11-47 | Basic and acidic residues | ||||
Sequence: RTKSQVIEEDYDDEQNTSAQHVESDKITAKTQHEEEE | ||||||
Compositional bias | 48-71 | Acidic residues | ||||
Sequence: EQDTGESEESSSEDDYEDQDDDDY | ||||||
Compositional bias | 78-102 | Basic residues | ||||
Sequence: KRKSRKRKPKSASNTSSKRQKKKPT | ||||||
Coiled coil | 305-349 | |||||
Sequence: LTQQAVNLEKNYLAKLSKQLSLEEKKKRPNNKTLEKLESTIAETQ | ||||||
Domain | 367-457 | SCD | ||||
Sequence: FVHRYKDVSDLIRSESMLHLSIWIKNYPEYFLKVTFLKYFGWLLSDNSVSVRLQVTKILPHLIIQNHNSKSTDNSAIRQVFERFKTKILEV | ||||||
Region | 1065-1150 | Disordered | ||||
Sequence: ENPEPNKKNIQKAKSNQTQREKAPLQPNSERETDHANTENNDPDIPMTIDLEPIEESSQNNSELAPIEEHPTVVDAIDNSDEITQD | ||||||
Compositional bias | 1073-1088 | Polar residues | ||||
Sequence: NIQKAKSNQTQREKAP | ||||||
Compositional bias | 1089-1103 | Basic and acidic residues | ||||
Sequence: LQPNSERETDHANTE |
Sequence similarities
Belongs to the SCC3 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,150
- Mass (Da)133,009
- Last updated1995-02-01 v1
- Checksum89688EA09485AC28
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 11-47 | Basic and acidic residues | ||||
Sequence: RTKSQVIEEDYDDEQNTSAQHVESDKITAKTQHEEEE | ||||||
Compositional bias | 48-71 | Acidic residues | ||||
Sequence: EQDTGESEESSSEDDYEDQDDDDY | ||||||
Compositional bias | 78-102 | Basic residues | ||||
Sequence: KRKSRKRKPKSASNTSSKRQKKKPT | ||||||
Sequence conflict | 939 | in Ref. 1; AAC49039 | ||||
Sequence: V → G | ||||||
Compositional bias | 1073-1088 | Polar residues | ||||
Sequence: NIQKAKSNQTQREKAP | ||||||
Compositional bias | 1089-1103 | Basic and acidic residues | ||||
Sequence: LQPNSERETDHANTE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U17918 EMBL· GenBank· DDBJ | AAC49039.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z46881 EMBL· GenBank· DDBJ | CAA86966.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006942 EMBL· GenBank· DDBJ | DAA08520.1 EMBL· GenBank· DDBJ | Genomic DNA |