Reviewed,
UniProtKB/Swiss-Prot P32908 (SMC1_YEAST)
Last modified
September 2, 2008.
Version 85.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Structural maintenance of chromosomes protein 1 Alternative name(s): DA-box protein SMC1 | ||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 1225 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| 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. |
| Subunit structure | Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1/SCC1 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. |
| Subcellular location | Nucleus. Note= Associates with chromatin. Before prophase it is scattered along chromosome arms. At anaphase, the MCD1 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. |
| Domain | The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC3, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable MCD1 protein, forming a ring structure. |
| Miscellaneous | Present with 5710 molecules/cell in log phase SD medium. |
| Sequence similarities | Belongs to the SMC family. SMC1 subfamily. |
Ontologies
Keywords | |
|---|---|
| Biological process | Cell cycle Cell division Mitosis |
| Cellular component | Nucleus |
| Domain | Coiled coil |
| Ligand | ATP-binding Nucleotide-binding |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Complete proteome |
Gene Ontology (GO) | |
| Biological process | double-strand break repair Inferred from mutant phenotype. Source: SGD mitotic sister chromatid cohesionInferred from mutant phenotype. Source: SGD |
| Cellular component | nuclear cohesin complex Ref.3 Inferred from direct assay. Source: SGD |
| Molecular function | AT DNA binding Inferred from direct assay. Source: SGD DNA secondary structure bindingInferred from direct assay. Source: SGD double-stranded DNA bindingInferred from direct assay. Source: SGD protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| CSM1 | P25651 | 2 | EBI-17402,EBI-22001 | |
| SMC3 | P47037 | 1 | EBI-17402,EBI-17423 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | |||||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1225 | 1225 | Structural maintenance of chromosomes protein 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Nucleotide binding | 33 – 40 | 8 | ATP Potential | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 490 – 678 | 189 | Flexible hinge | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Coiled coil | 173 – 489 | 317 | Potential | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Coiled coil | 679 – 1063 | 385 | Potential | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Motif | 1057 – 1061 | 5 | Nuclear localization signal Potential | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Compositional bias | 1129 – 1164 | 36 | Ala/Asp-rich (DA-box) | ||||||||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 327 | 1 | Phosphoserine | ||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 173 | 1 | S → L in temperature-sensitive mutant SMC1-2 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 458 | 1 | N → D in temperature-sensitive mutant SMC1-1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 4 – 11 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 17 – 22 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 27 – 32 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 39 – 49 | 11 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 63 – 65 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 91 – 100 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 103 – 112 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 117 – 121 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 124 – 126 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 128 – 137 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 142 – 144 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 156 – 159 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 162 – 167 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 271 – 284 | 14 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 299 – 302 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 317 – 320 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 329 – 331 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 334 – 349 | 16 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 355 – 361 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 362 – 365 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 368 – 381 | 14 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 386 – 391 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 395 – 398 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "SMC1: an essential yeast gene encoding a putative head-rod-tail protein is required for nuclear division and defines a new ubiquitous protein family." Strunnikov A.V., Larionov V.L., Koshland D. J. Cell Biol. 123:1635-1648(1993) [PubMed: 8276886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, MUTANTS SMC1-1 AND SMC1-2. |
| [2] | "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T. Nat. Genet. 10:261-268(1995) [PubMed: 7670463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972. |
| [3] | "Yeast cohesin complex requires a conserved protein, Eco1p(Ctf7), to establish cohesion between sister chromatids during DNA replication." Toth A., Ciosk R., Uhlmann F., Galova M., Schleiffer A., Nasmyth K. Genes Dev. 13:320-333(1999) [PubMed: 9990856] [Abstract] Cited for: IDENTIFICATION IN A COHESIN COMPLEX WITH SMC3; IRR1 AND MCD1, INTERACTION OF THE COHESIN COMPLEX WITH SCC2. |
| [4] | "Molecular architecture of SMC proteins and the yeast cohesin complex." Haering C.H., Loewe J., Hochwagen A., Nasmyth K. Mol. Cell 9:773-788(2002) [PubMed: 11983169] [Abstract] Cited for: IDENTIFICATION IN A COHESIN COMPLEX WITH SMC3; MCD1 AND IRR1, STRUCTURE. |
| [5] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [6] | "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| L00602 Unassigned DNA. Translation: AAA16595.1. D50617 Genomic DNA. Translation: BAA09230.1. | |||||||||||||
| PIR | A49464. | ||||||||||||
| RefSeq | NP_116647.1. | ||||||||||||
3D structure databases | |||||||||||||
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| SMR | P32908. Positions 1048-1223. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP:2982N. | ||||||||||||
| IntAct | P32908. | ||||||||||||
Proteomic databases | |||||||||||||
| PeptideAtlas | P32908. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | YFL008W. Saccharomyces cerevisiae. [Contig view] | ||||||||||||
| GeneID | 850540. | ||||||||||||
| GenomeReviews | Gene locus YFL008W in contig D50617_GR. | ||||||||||||
| KEGG | sce:YFL008W. | ||||||||||||
| NMPDR | fig|4932.3.peg.2278. | ||||||||||||
Organism-specific databases | |||||||||||||
| CYGD | YFL008w. | ||||||||||||
| SGD | S000001886. SMC1. | ||||||||||||
| Yeast-GFP | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | P32908. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P32908. | ||||||||||||
| GermOnline | YFL008W. Saccharomyces cerevisiae. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR003395. RecF/RecN/SMC_N. IPR010935. SMC_hinge. [Graphical view] | ||||||||||||
| Pfam | PF06470. SMC_hinge. 1 hit. PF02463. SMC_N. 1 hit. [Graphical view] | ||||||||||||
| ProDom | PD000006. ABC_transporter. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| BLOCKS | Search... | ||||||||||||
Other Resources | |||||||||||||
| LinkHub | P32908. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | SMC1_YEAST | ||||||||
| Accession | Primary (citable) accession number: P32908 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome VI Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names |

Clusters with


