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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: 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

GO - Molecular functioni

  • chromatin binding Source: SGD

GO - Biological processi

  • apoptotic process Source: SGD
  • cell division Source: UniProtKB-KW
  • cellular response to DNA damage stimulus Source: SGD
  • DNA unwinding involved in DNA replication Source: SGD
  • double-strand break repair Source: SGD
  • establishment of mitotic sister chromatid cohesion Source: SGD
  • meiotic sister chromatid cohesion, centromeric Source: GO_Central
  • mitotic chromosome condensation Source: SGD
  • protein acetylation Source: UniProtKB
  • 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
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL003W.
SGDiS000002161. MCD1.

Subcellular locationi

  • Nucleus 3 Publications
  • Chromosome 2 Publications
  • Chromosomecentromere 1 Publication

  • 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.1 Publication

GO - Cellular componenti

  • chromosome, centromeric region Source: UniProtKB-SubCell
  • condensed nuclear chromosome Source: SGD
  • mitochondrion Source: SGD
  • nuclear meiotic cohesin complex Source: GO_Central
  • nuclear mitotic cohesin complex Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

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.
PRIDEiQ12158.
TopDownProteomicsiQ12158.

PTM databases

iPTMnetiQ12158.

Miscellaneous databases

PMAP-CutDBQ12158.

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. 124 interactors.
DIPiDIP-5812N.
IntActiQ12158. 36 interactors.
MINTiMINT-627334.

Structurei

Secondary structure

1566
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 28Combined sources3
Helixi44 – 51Combined sources8
Turni52 – 54Combined sources3
Beta strandi56 – 58Combined sources3
Helixi69 – 100Combined sources32
Beta strandi134 – 138Combined sources5
Helixi484 – 495Combined sources12
Helixi504 – 509Combined sources6
Helixi522 – 537Combined sources16
Beta strandi539 – 544Combined sources6
Beta strandi551 – 555Combined sources5
Helixi557 – 559Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W1WX-ray2.90E/F/G/H451-564[»]
4UX3X-ray3.30B1-115[»]
5FRPX-ray2.90C/D116-159[»]
5FRSX-ray4.07C126-142[»]
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.
OMAiGPLAQIW.
OrthoDBiEOG092C11R6.

Family and domain databases

Gene3Di1.10.10.580. 1 hit.
InterProiIPR023093. Rad21/Rec8_C.
IPR006909. Rad21/Rec8_C_eu.
IPR006910. Rad21_Rec8_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF04824. Rad21_Rec8. 1 hit.
PF04825. Rad21_Rec8_N. 1 hit.
[Graphical view]
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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W1WX-ray2.90E/F/G/H451-564[»]
4UX3X-ray3.30B1-115[»]
5FRPX-ray2.90C/D116-159[»]
5FRSX-ray4.07C126-142[»]
ProteinModelPortaliQ12158.
SMRiQ12158.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32051. 124 interactors.
DIPiDIP-5812N.
IntActiQ12158. 36 interactors.
MINTiMINT-627334.

PTM databases

iPTMnetiQ12158.

Proteomic databases

MaxQBiQ12158.
PRIDEiQ12158.
TopDownProteomicsiQ12158.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YDL003W.
SGDiS000002161. MCD1.

Phylogenomic databases

HOGENOMiHOG000141751.
InParanoidiQ12158.
KOiK06670.
OMAiGPLAQIW.
OrthoDBiEOG092C11R6.

Enzyme and pathway databases

BioCyciYEAST:G3O-29434-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ12158.
PMAP-CutDBQ12158.
PROiQ12158.

Family and domain databases

Gene3Di1.10.10.580. 1 hit.
InterProiIPR023093. Rad21/Rec8_C.
IPR006909. Rad21/Rec8_C_eu.
IPR006910. Rad21_Rec8_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF04824. Rad21_Rec8. 1 hit.
PF04825. Rad21_Rec8_N. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 146 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.