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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: -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

Miscellaneous

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

GO - Molecular functioni

  • chromatin binding Source: SGD
  • protein kinase binding Source: SGD

GO - Biological processi

Keywordsi

Biological processCell 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
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL003W
SGDiS000002161 MCD1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi175S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-263. 1 Publication1
Mutagenesisi180R → D: Abolishes cleavage by ESP1; when associated with D-268. 1 Publication1
Mutagenesisi210K → R: Loss of acetylation by ECO1. 1 Publication1
Mutagenesisi252K → R: No effect on acetylation by ECO1. 1 Publication1
Mutagenesisi263S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-175. 1 Publication1
Mutagenesisi268R → D: Abolishes first cleavage by ESP1. Abolishes all cleavage by ESP1; when associated with D-180. 1 Publication1
Mutagenesisi290K → R: No effect on acetylation by ECO1. 1 Publication1
Mutagenesisi310K → R: No effect on acetylation by ECO1. 1 Publication1
Mutagenesisi319K → R: No effect on acetylation by ECO1. 1 Publication1
Mutagenesisi324K → R: No effect on acetylation by ECO1. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000978811 – 566Sister chromatid cohesion protein 1Add BLAST566

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei161PhosphoserineCombined sources1
Modified residuei175Phosphoserine; by CDC51 Publication1
Modified residuei210N6-acetyllysine; by ECO11 Publication1
Modified residuei263Phosphoserine; by CDC51 Publication1
Modified residuei307PhosphoserineCombined sources1
Modified residuei354PhosphothreonineCombined sources1

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 ESP1.2 Publications
Acetylated by ECO1.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei180 – 181Cleavage; by ESP12
Sitei268 – 269Cleavage; by ESP12

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ12158
PaxDbiQ12158
PRIDEiQ12158
TopDownProteomicsiQ12158

PTM databases

iPTMnetiQ12158

Miscellaneous databases

PMAP-CutDBiQ12158

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi32051, 335 interactors
ComplexPortaliCPX-1867 Nuclear mitotic cohesin complex
DIPiDIP-5812N
ELMiQ12158
IntActiQ12158, 36 interactors
MINTiQ12158
STRINGi4932.YDL003W

Structurei

Secondary structure

1566
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ12158
SMRiQ12158
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12158

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi258 – 261Poly-Asp4

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

HOGENOMiHOG000141751
InParanoidiQ12158
KOiK06670
OMAiGAWAERE
OrthoDBiEOG092C11R6

Family and domain databases

Gene3Di1.10.10.580, 1 hit
InterProiView protein in InterPro
IPR006909 Rad21/Rec8_C_eu
IPR006910 Rad21_Rec8_N
IPR023093 ScpA-like_C
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF04824 Rad21_Rec8, 1 hit
PF04825 Rad21_Rec8_N, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit

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:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiSCC1_YEAST
AccessioniPrimary (citable) accession number: Q12158
Secondary accession number(s): D6VRY5, Q05325
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: November 1, 1996
Last modified: September 12, 2018
This is version 163 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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