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Q12158 (SCC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sister chromatid cohesion protein 1
Gene names
Name:MCD1
Synonyms:PDS3, RHC21, SCC1
Ordered Locus Names:YDL003W
ORF Names:YD8119.04
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleavable component of the cohesin complex involved in chromosome cohesion during cell cycle. 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 metaphase-anaphase transition, this protein is cleaved by ESP1 and dissociates from chromatin, allowing sister chromatids to segregate. Ref.1 Ref.2 Ref.5 Ref.7

Subunit structure

Interacts directly with IRR1/SCC3 in cohesin complex. Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1/SCC1 which link them, and IRR1, which interacts with MCD1. The cohesin complex also interacts with SCC2, which is required for its association with chromosomes. Ref.6 Ref.9

Subcellular location

Nucleus. Chromosome. Chromosomecentromere. 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, it is cleaved by ESP1, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. Ref.1 Ref.2 Ref.6

Domain

The C-terminal part associates with the head of SMC1, while the N-terminal part binds to the head of SMC3.

Post-translational modification

Cleaved by ESP1 at the onset of anaphase.

Phosphorylated by CDC5/Polo-like kinase at the onset of anaphase. Phosphorylation takes places at proximity to cleavage sites and is required for an efficient cleavage by ESP1. Ref.8

Acetylated by ECO1. Ref.10

Miscellaneous

Present with 1040 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the rad21 family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Chromosome partition
Mitosis
   Cellular componentCentromere
Chromosome
Nucleus
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA unwinding involved in DNA replication

Inferred from mutant phenotype PubMed 24062159. Source: SGD

apoptotic process

Inferred from mutant phenotype PubMed 18321989. Source: SGD

cellular response to DNA damage stimulus

Inferred from mutant phenotype PubMed 18614046. Source: SGD

double-strand break repair

Inferred from mutant phenotype PubMed 11448778PubMed 23178808. Source: SGD

establishment of mitotic sister chromatid cohesion

Inferred from mutant phenotype PubMed 16962805. Source: SGD

mitotic chromosome condensation

Inferred from mutant phenotype Ref.2. Source: SGD

protein acetylation

Inferred from direct assay Ref.10. Source: UniProtKB

   Cellular_componentchromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

condensed nuclear chromosome

Inferred from direct assay PubMed 18614046. Source: SGD

mitochondrion

Inferred from direct assay PubMed 18321989. Source: SGD

nuclear mitotic cohesin complex

Inferred from direct assay Ref.6. Source: SGD

nucleus

Inferred from direct assay PubMed 15282802. Source: SGD

   Molecular_functionchromatin binding

Inferred from direct assay PubMed 18614046Ref.6. Source: SGD

protein binding

Inferred from physical interaction PubMed 10882066PubMed 11805826Ref.9PubMed 16429126PubMed 17660750PubMed 21139566. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 566566Sister chromatid cohesion protein 1
PRO_0000097881

Regions

Compositional bias258 – 2614Poly-Asp

Sites

Site180 – 1812Cleavage; by ESP1
Site268 – 2692Cleavage; by ESP1

Amino acid modifications

Modified residue1611Phosphoserine Ref.12
Modified residue1751Phosphoserine; by CDC5 Ref.8
Modified residue2101N6-acetyllysine; by ECO1 Ref.10
Modified residue2631Phosphoserine; by CDC5 Ref.8
Modified residue3071Phosphoserine Ref.12
Modified residue3541Phosphothreonine Ref.12

Experimental info

Mutagenesis1751S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-263. Ref.8
Mutagenesis1801R → D: Abolishes cleavage by ESP1; when associated with D-268. Ref.7
Mutagenesis2101K → R: Loss of acetylation by ECO1. Ref.10
Mutagenesis2521K → R: No effect on acetylation by ECO1. Ref.10
Mutagenesis2631S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-175. Ref.8
Mutagenesis2681R → D: Abolishes first cleavage by ESP1. Abolishes all cleavage by ESP1; when associated with D-180. Ref.7
Mutagenesis2901K → R: No effect on acetylation by ECO1. Ref.10
Mutagenesis3101K → R: No effect on acetylation by ECO1. Ref.10
Mutagenesis3191K → R: No effect on acetylation by ECO1. Ref.10
Mutagenesis3241K → R: No effect on acetylation by ECO1. Ref.10

Secondary structure

............. 566
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12158 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: EB6C7CA33BAC208F

FASTA56663,290
        10         20         30         40         50         60 
MVTENPQRLT VLRLATNKGP LAQIWLASNM SNIPRGSVIQ THIAESAKEI AKASGCDDES 

        70         80         90        100        110        120 
GDNEYITLRT SGELLQGIVR VYSKQATFLL TDIKDTLTKI SMLFKTSQKM TSTVNRLNTV 

       130        140        150        160        170        180 
TRVHQLMLED AVTEREVLVT PGLEFLDDTT IPVGLMAQEN SMERKVQGAA PWDTSLEVGR 

       190        200        210        220        230        240 
RFSPDEDFEH NNLSSMNLDF DIEEGPITSK SWEEGTRQSS RNFDTHENYI QDDDFPLDDA 

       250        260        270        280        290        300 
GTIGWDLGIT EKNDQNNDDD DNSVEQGRRL GESIMSEEPT DFGFDLDIEK EAPAGNIDTI 

       310        320        330        340        350        360 
TDAMTESQPK QTGTRRNSKL LNTKSIQIDE ETENSESIAS SNTYKEERSN NLLTPQPTNF 

       370        380        390        400        410        420 
TTKRLWSEIT ESMSYLPDPI LKNFLSYESL KKRKIHNGRE GSIEEPELNV SLNLTDDVIS 

       430        440        450        460        470        480 
NAGTNDNSFN ELTDNMSDFV PIDAGLNEAP FPEENIIDAK TRNEQTTIQT EKVRPTPGEV 

       490        500        510        520        530        540 
ASKAIVQMAK ILRKELSEEK EVIFTDVLKS QANTEPENIT KREASRGFFD ILSLATEGCI 

       550        560 
GLSQTEAFGN IKIDAKPALF ERFINA 

« Hide

References

« Hide 'large scale' references
[1]"Cohesins: chromosomal proteins that prevent premature separation of sister chromatids."
Michaelis C., Ciosk R., Nasmyth K.
Cell 91:35-45(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
Strain: ATCC 200060 / W303.
[2]"A direct link between sister chromatid cohesion and chromosome condensation revealed through the analysis of MCD1 in S. cerevisiae."
Guacci V., Koshland D., Strunnikov A.V.
Cell 91:47-57(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
Strain: ATCC 204508 / S288c.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"The RHC21 gene of budding yeast, a homologue of the fission yeast rad21+ gene, is essential for chromosome segregation."
Heo S.-J., Tatebayashi K., Kato J., Ikeda H.
Mol. Gen. Genet. 257:149-156(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH IRR1, IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1; SMC3 AND IRR1, INTERACTION OF THE COHESIN COMPLEX WITH SCC2.
[7]"Sister-chromatid separation at anaphase onset is promoted by cleavage of the cohesin subunit Scc1."
Uhlmann F., Lottspeich F., Nasmyth K.
Nature 400:37-42(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY ESP1, FUNCTION, MUTAGENESIS OF ARG-180 AND ARG-268.
[8]"Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast."
Alexandru G., Uhlmann F., Mechtler K., Poupart M.-A., Nasmyth K.
Cell 105:459-472(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-175 AND SER-263 BY CDC5, MUTAGENESIS OF SER-175 AND SER-263.
[9]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1; SMC3 AND IRR1, STRUCTURE.
[10]"Eco1 is a novel acetyltransferase that can acetylate proteins involved in cohesion."
Ivanov D., Schleiffer A., Eisenhaber F., Mechtler K., Haering C.H., Nasmyth K.
Curr. Biol. 12:323-328(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-210, MUTAGENESIS OF LYS-210; LYS-252; LYS-290; LYS-310; LYS-319 AND LYS-324.
[11]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-307 AND THR-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y14280 Genomic DNA. Translation: CAA74657.1.
U23759 Genomic DNA. Translation: AAB38803.1.
Z48008 Genomic DNA. Translation: CAA88058.1.
Z48432 Genomic DNA. Translation: CAA88356.1.
Z74051 Genomic DNA. Translation: CAA98559.1.
BK006938 Genomic DNA. Translation: DAA11845.1.
PIRS50979.
RefSeqNP_010281.1. NM_001180062.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W1WX-ray2.90E/F/G/H451-564[»]
ProteinModelPortalQ12158.
SMRQ12158. Positions 483-560.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32051. 120 interactions.
DIPDIP-5812N.
IntActQ12158. 36 interactions.
MINTMINT-627334.

Proteomic databases

MaxQBQ12158.
PaxDbQ12158.
PeptideAtlasQ12158.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL003W; YDL003W; YDL003W.
GeneID851561.
KEGGsce:YDL003W.

Organism-specific databases

CYGDYDL003w.
SGDS000002161. MCD1.

Phylogenomic databases

eggNOGNOG249424.
HOGENOMHOG000141751.
KOK06670.
OMAIWLASNM.
OrthoDBEOG7KSXM4.

Enzyme and pathway databases

BioCycYEAST:G3O-29434-MONOMER.

Gene expression databases

GenevestigatorQ12158.

Family and domain databases

Gene3D1.10.10.580. 1 hit.
InterProIPR023093. Rad21/Rec8_C.
IPR006909. Rad21/Rec8_C_eu.
IPR006910. Rad21_Rec8_N.
[Graphical view]
PfamPF04824. Rad21_Rec8. 1 hit.
PF04825. Rad21_Rec8_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ12158.
NextBio968995.
PMAP-CutDBQ12158.

Entry information

Entry nameSCC1_YEAST
AccessionPrimary (citable) accession number: Q12158
Secondary accession number(s): D6VRY5, Q05325
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references