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Q12158

- SCC1_YEAST

UniProt

Q12158 - SCC1_YEAST

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Protein

Sister chromatid cohesion protein 1

Gene

MCD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei180 – 1812Cleavage; by ESP1
Sitei268 – 2692Cleavage; by ESP1

GO - Molecular functioni

  1. chromatin binding Source: SGD

GO - Biological processi

  1. apoptotic process Source: SGD
  2. cellular response to DNA damage stimulus Source: SGD
  3. DNA unwinding involved in DNA replication Source: SGD
  4. double-strand break repair Source: SGD
  5. establishment of mitotic sister chromatid cohesion Source: SGD
  6. mitotic chromosome condensation Source: SGD
  7. protein acetylation Source: UniProtKB
  8. replication-born double-strand break repair via sister chromatid exchange Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Mitosis

Enzyme and pathway databases

BioCyciYEAST:G3O-29434-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Sister chromatid cohesion protein 1
Gene namesi
Name:MCD1
Synonyms:PDS3, RHC21, SCC1
Ordered Locus Names:YDL003W
ORF Names:YD8119.04
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDL003w.
SGDiS000002161. MCD1.

Subcellular locationi

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.

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB-KW
  2. condensed nuclear chromosome Source: SGD
  3. mitochondrion Source: SGD
  4. nuclear mitotic cohesin complex Source: SGD
  5. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi175 – 1751S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-263. 1 Publication
Mutagenesisi180 – 1801R → D: Abolishes cleavage by ESP1; when associated with D-268. 1 Publication
Mutagenesisi210 – 2101K → R: Loss of acetylation by ECO1. 1 Publication
Mutagenesisi252 – 2521K → R: No effect on acetylation by ECO1. 1 Publication
Mutagenesisi263 – 2631S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-175. 1 Publication
Mutagenesisi268 – 2681R → D: Abolishes first cleavage by ESP1. Abolishes all cleavage by ESP1; when associated with D-180. 1 Publication
Mutagenesisi290 – 2901K → R: No effect on acetylation by ECO1. 1 Publication
Mutagenesisi310 – 3101K → R: No effect on acetylation by ECO1. 1 Publication
Mutagenesisi319 – 3191K → R: No effect on acetylation by ECO1. 1 Publication
Mutagenesisi324 – 3241K → R: No effect on acetylation by ECO1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 566566Sister chromatid cohesion protein 1PRO_0000097881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei161 – 1611Phosphoserine1 Publication
Modified residuei175 – 1751Phosphoserine; by CDC51 Publication
Modified residuei210 – 2101N6-acetyllysine; by ECO11 Publication
Modified residuei263 – 2631Phosphoserine; by CDC51 Publication
Modified residuei307 – 3071Phosphoserine1 Publication
Modified residuei354 – 3541Phosphothreonine1 Publication

Post-translational modificationi

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 ESP1.3 Publications
Acetylated by ECO1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ12158.
PaxDbiQ12158.
PeptideAtlasiQ12158.

Miscellaneous databases

PMAP-CutDBQ12158.

Expressioni

Gene expression databases

GenevestigatoriQ12158.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IRR1P405415EBI-16655,EBI-16667
SMC1P329088EBI-16655,EBI-17402
SMC3P4703713EBI-16655,EBI-17423

Protein-protein interaction databases

BioGridi32051. 120 interactions.
DIPiDIP-5812N.
IntActiQ12158. 36 interactions.
MINTiMINT-627334.

Structurei

Secondary structure

1
566
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi484 – 49512
Helixi504 – 5096
Helixi522 – 53716
Beta strandi539 – 5446
Beta strandi551 – 5555
Helixi557 – 5593

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W1WX-ray2.90E/F/G/H451-564[»]
ProteinModelPortaliQ12158.
SMRiQ12158. Positions 483-560.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12158.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi258 – 2614Poly-Asp

Domaini

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

Sequence similaritiesi

Belongs to the rad21 family.Curated

Phylogenomic databases

eggNOGiNOG249424.
HOGENOMiHOG000141751.
InParanoidiQ12158.
KOiK06670.
OMAiIWLASNM.
OrthoDBiEOG7KSXM4.

Family and domain databases

Gene3Di1.10.10.580. 1 hit.
InterProiIPR023093. Rad21/Rec8_C.
IPR006909. Rad21/Rec8_C_eu.
IPR006910. Rad21_Rec8_N.
[Graphical view]
PfamiPF04824. Rad21_Rec8. 1 hit.
PF04825. Rad21_Rec8_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12158-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVTENPQRLT VLRLATNKGP LAQIWLASNM SNIPRGSVIQ THIAESAKEI
60 70 80 90 100
AKASGCDDES GDNEYITLRT SGELLQGIVR VYSKQATFLL TDIKDTLTKI
110 120 130 140 150
SMLFKTSQKM TSTVNRLNTV TRVHQLMLED AVTEREVLVT PGLEFLDDTT
160 170 180 190 200
IPVGLMAQEN SMERKVQGAA PWDTSLEVGR RFSPDEDFEH NNLSSMNLDF
210 220 230 240 250
DIEEGPITSK SWEEGTRQSS RNFDTHENYI QDDDFPLDDA GTIGWDLGIT
260 270 280 290 300
EKNDQNNDDD DNSVEQGRRL GESIMSEEPT DFGFDLDIEK EAPAGNIDTI
310 320 330 340 350
TDAMTESQPK QTGTRRNSKL LNTKSIQIDE ETENSESIAS SNTYKEERSN
360 370 380 390 400
NLLTPQPTNF TTKRLWSEIT ESMSYLPDPI LKNFLSYESL KKRKIHNGRE
410 420 430 440 450
GSIEEPELNV SLNLTDDVIS NAGTNDNSFN ELTDNMSDFV PIDAGLNEAP
460 470 480 490 500
FPEENIIDAK TRNEQTTIQT EKVRPTPGEV ASKAIVQMAK ILRKELSEEK
510 520 530 540 550
EVIFTDVLKS QANTEPENIT KREASRGFFD ILSLATEGCI GLSQTEAFGN
560
IKIDAKPALF ERFINA
Length:566
Mass (Da):63,290
Last modified:November 1, 1996 - v1
Checksum:iEB6C7CA33BAC208F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS50979.
RefSeqiNP_010281.1. NM_001180062.1.

Genome annotation databases

EnsemblFungiiYDL003W; YDL003W; YDL003W.
GeneIDi851561.
KEGGisce:YDL003W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S50979.
RefSeqi NP_010281.1. NM_001180062.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1W1W X-ray 2.90 E/F/G/H 451-564 [» ]
ProteinModelPortali Q12158.
SMRi Q12158. Positions 483-560.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32051. 120 interactions.
DIPi DIP-5812N.
IntActi Q12158. 36 interactions.
MINTi MINT-627334.

Proteomic databases

MaxQBi Q12158.
PaxDbi Q12158.
PeptideAtlasi Q12158.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDL003W ; YDL003W ; YDL003W .
GeneIDi 851561.
KEGGi sce:YDL003W.

Organism-specific databases

CYGDi YDL003w.
SGDi S000002161. MCD1.

Phylogenomic databases

eggNOGi NOG249424.
HOGENOMi HOG000141751.
InParanoidi Q12158.
KOi K06670.
OMAi IWLASNM.
OrthoDBi EOG7KSXM4.

Enzyme and pathway databases

BioCyci YEAST:G3O-29434-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q12158.
NextBioi 968995.
PMAP-CutDB Q12158.

Gene expression databases

Genevestigatori Q12158.

Family and domain databases

Gene3Di 1.10.10.580. 1 hit.
InterProi IPR023093. Rad21/Rec8_C.
IPR006909. Rad21/Rec8_C_eu.
IPR006910. Rad21_Rec8_N.
[Graphical view ]
Pfami PF04824. Rad21_Rec8. 1 hit.
PF04825. Rad21_Rec8_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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].

Entry informationi

Entry nameiSCC1_YEAST
AccessioniPrimary (citable) accession number: Q12158
Secondary accession number(s): D6VRY5, Q05325
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1040 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3