P32908 (SMC1_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 117.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 (strain ATCC 204508 / S288c) (Baker's yeast) | ||||||
| Taxonomic identifier | 559292 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 1225 AA. |
| Sequence status | Complete. |
| 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. Ref.4 |
| Subcellular location | Nucleus. Chromosome. 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. Ref.6 |
| Sequence similarities | Belongs to the SMC family. SMC1 subfamily. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| itself | 8 | EBI-17402,EBI-17402 | ||
| DYN1 | P36022 | 3 | EBI-17402,EBI-6230 | |
| KAR3 | P17119 | 4 | EBI-17402,EBI-9499 | |
| MCD1 | Q12158 | 7 | EBI-17402,EBI-16655 | |
| NNF1 | P47149 | 6 | EBI-17402,EBI-12098 | |
| NNF2 | P53253 | 4 | EBI-17402,EBI-23229 | |
| SMC2 | P38989 | 3 | EBI-17402,EBI-17412 | |
| SMC3 | P47037 | 13 | EBI-17402,EBI-17423 | |
| SMC3 | Q9UQE7 | 4 | EBI-17402,EBI-80718 | From a different organism. |
| SPC42 | P36094 | 3 | EBI-17402,EBI-17777 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1225 | 1225 | Structural maintenance of chromosomes protein 1 | PRO_0000119011 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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 Ref.7 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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] | Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c. |
| [4] | "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. |
| [5] | "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. |
| [6] | "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]. |
| [7] | "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 | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | L00602 Unassigned DNA. Translation: AAA16595.1. D50617 Genomic DNA. Translation: BAA09230.1. BK006940 Genomic DNA. Translation: DAA12432.1. | ||||||||||||
| PIR | A49464. | ||||||||||||
| RefSeq | NP_116647.1. NM_001179958.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P32908. | ||||||||||||
| SMR | P32908. Positions 2-205, 517-674, 1048-1223. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-2982N. | ||||||||||||
| IntAct | P32908. 27 interactions. | ||||||||||||
| MINT | MINT-434606. | ||||||||||||
| STRING | P32908. | ||||||||||||
Proteomic databases | |||||||||||||
| PeptideAtlas | P32908. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblFungi | YFL008W; YFL008W; YFL008W. | ||||||||||||
| GeneID | 850540. | ||||||||||||
| KEGG | sce:YFL008W. | ||||||||||||
| NMPDR | fig|4932.3.peg.2278. | ||||||||||||
Organism-specific databases | |||||||||||||
| CYGD | YFL008w. | ||||||||||||
| SGD | S000001886. SMC1. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | fuNOG06246. | ||||||||||||
| GeneTree | EFGT00050000000440. | ||||||||||||
| HOGENOM | HBG559513. | ||||||||||||
| OMA | YQPSPFF. | ||||||||||||
| OrthoDB | EOG42VCQD. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P32908. | ||||||||||||
| Genevestigator | P32908. | ||||||||||||
| GermOnline | YFL008W. Saccharomyces cerevisiae. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR003395. RecF/RecN/SMC. IPR024704. SMC. IPR010935. SMC_hinge. [Graphical view] | ||||||||||||
| KO | K06636. | ||||||||||||
| Pfam | PF06470. SMC_hinge. 1 hit. PF02463. SMC_N. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF005719. SMC. 1 hit. | ||||||||||||
| SMART | SM00968. SMC_hinge. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF75553. SMC_hinge. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| NextBio | 966301. | ||||||||||||
Entry information
| Entry name | SMC1_YEAST | ||||||||
| Accession | Primary (citable) accession number: P32908 Secondary accession number(s): D6VTM2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome VI Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with