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Protein

Cell division control protein 53

Gene

CDC53

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

Functioni

Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The SCF complex associates with CDC34 as the E2 ubiquitin-conjugating enzyme. The functional specificity of the SCF complex depends on the type of F-box protein. SCF(CDC4) controls the G1-to-S phase transition; it directs ubiquitination of the phosphorylated CDK inhibitor SIC1 and of CDC6. SCF(CDC4) directs ubiquitination of GCN4. SCF(GRR1) directs ubiquitination of phosphorylated CLN1, CLN2 and GIC2. SCF(MET30) directs ubiquitination of MET4. SCF(DIA2) is specifically involved in the pheromone induced degradation of phosphorylated TEC1. SCF(MDM30) seems to direct ubiquitination of FZ01. Involved in the regulation of methionine biosynthesis genes.8 Publications

Miscellaneous

Present with 377 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

  • DNA replication origin binding Source: SGD
  • protein binding, bridging Source: SGD
  • ubiquitin protein ligase binding Source: GO_Central

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • G1/S transition of mitotic cell cycle Source: SGD
  • G2/M transition of mitotic cell cycle Source: SGD
  • protein ubiquitination Source: GOC
  • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: SGD
  • ubiquitin-dependent protein catabolic process Source: SGD

Keywordsi

Biological processCell cycle, Cell division

Enzyme and pathway databases

BioCyciYEAST:G3O-29530-MONOMER
ReactomeiR-SCE-110314 Recognition of DNA damage by PCNA-containing replication complex
R-SCE-174113 SCF-beta-TrCP mediated degradation of Emi1
R-SCE-5696394 DNA Damage Recognition in GG-NER
R-SCE-5696395 Formation of Incision Complex in GG-NER
R-SCE-5696400 Dual Incision in GG-NER
R-SCE-6781823 Formation of TC-NER Pre-Incision Complex
R-SCE-6782135 Dual incision in TC-NER
R-SCE-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-SCE-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-SCE-8951664 Neddylation
R-SCE-917937 Iron uptake and transport
R-SCE-983168 Antigen processing: Ubiquitination & Proteasome degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division control protein 53
Alternative name(s):
Cullin-A
E3 ubiquitin ligase complex SCF subunit CDC53
Gene namesi
Name:CDC53
Ordered Locus Names:YDL132W
ORF Names:D2190
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL132W
SGDiS000002290 CDC53

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

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi488R → C: Prevents CDC34/UBC3 interaction. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001198051 – 815Cell division control protein 53Add BLAST815

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki760Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)By similarity

Post-translational modificationi

Neddylated; enhancing the ubiquitin-ligase activity.By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ12018
PaxDbiQ12018
PRIDEiQ12018

PTM databases

iPTMnetiQ12018

Interactioni

Subunit structurei

Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes formed of CUL1, SKP1/HRT1, RBX1 and a variable F-box domain-containing protein as substrate-specific adapter. Component of the SCF(CDC4) complex containing CDC4. Component of the SCF(MET30) complex containing MET30. Component of the SCF(GRR1) complex containig GRR1. Component of the probable SCF(DIA2) complex containing DIA2. Component of the probable SCF(YDR131C) complex containing YDR131C. Component of the probable SCF(YDR306C) complex containing YDR306C. Component of the probable SCF(YLR224W) complex containing YLR224W. Component of the probable SCF(YJL149W) complex containing YJL149W. Component of the probable SCF(YNL311C) complex containing YNL311C. Component of the probable SCF(MDM30) complex containing MDM30. Component of the probable SCF(UFO1) complex containing UFO1. Component of the probable SCF(HRT3) complex containing HRT3. Component of the probable SCF(YBR280C) complex containing YBR280C. Component of the probable SCF(YBR352W) complex containing YBR352W. Interacts with DCN1, YBR280C, YLR224W and YLR352W. The unneddylated form interacts with LAG2/CAND1 and the interaction mediates the exchange of the F-box substrate-specific subunit.8 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein binding, bridging Source: SGD
  • ubiquitin protein ligase binding Source: GO_Central

Protein-protein interaction databases

BioGridi31930, 501 interactors
DIPiDIP-1234N
IntActiQ12018, 73 interactors
MINTiQ12018
STRINGi4932.YDL132W

Structurei

Secondary structure

1815
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi735 – 762Combined sources28
Beta strandi763 – 766Combined sources4
Helixi767 – 778Combined sources12
Turni779 – 781Combined sources3
Helixi786 – 798Combined sources13
Beta strandi801 – 804Combined sources4
Beta strandi808 – 813Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3O2PX-ray2.23E730-815[»]
3O6BX-ray3.10B/D/F/H/J742-815[»]
ProteinModelPortaliQ12018
SMRiQ12018
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12018

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 280Required for interaction with SKP1/CBF3D and F-box proteinAdd BLAST272
Regioni448 – 748Required for interaction with CDC34/UBC3Add BLAST301

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00760000119212
HOGENOMiHOG000176713
InParanoidiQ12018
KOiK03347
OMAiTTHKHIE
OrthoDBiEOG092C1L4K

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR016157 Cullin_CS
IPR016158 Cullin_homology
IPR036317 Cullin_homology_sf
IPR001373 Cullin_N
IPR019559 Cullin_neddylation_domain
IPR016159 Cullin_repeat-like_dom_sf
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00888 Cullin, 1 hit
PF10557 Cullin_Nedd8, 1 hit
SMARTiView protein in SMART
SM00182 CULLIN, 1 hit
SM00884 Cullin_Nedd8, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF74788 SSF74788, 1 hit
SSF75632 SSF75632, 1 hit
PROSITEiView protein in PROSITE
PS01256 CULLIN_1, 1 hit
PS50069 CULLIN_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q12018-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSETLPRSDD LEATWNFIEP GINQILGNEK NQASTSKRVY KILSPTMYME
60 70 80 90 100
VYTAIYNYCV NKSRSSGHFS TDSRTGQSTI LVGSEIYEKL KNYLKNYILN
110 120 130 140 150
FKQSNSETFL QFYVKRWKRF TIGAIFLNHA FDYMNRYWVQ KERSDGKRHI
160 170 180 190 200
FDVNTLCLMT WKEVMFDPSK DVLINELLDQ VTLGREGQII QRSNISTAIK
210 220 230 240 250
SLVALGIDPQ DLKKLNLNVY IQVFEKPFLK KTQEYYTQYT NDYLEKHSVT
260 270 280 290 300
EYIFEAHEII KREEKAMTIY WDDHTKKPLS MALNKVLITD HIEKLENEFV
310 320 330 340 350
VLLDARDIEK ITSLYALIRR DFTLIPRMAS VFENYVKKTG ENEISSLLAM
360 370 380 390 400
HKHNIMKNEN ANPKKLALMT AHSLSPKDYI KKLLEVHDIF SKIFNESFPD
410 420 430 440 450
DIPLAKALDN ACGAFININE FALPAGSPKS ATSKTSEMLA KYSDILLKKA
460 470 480 490 500
TKPEVASDMS DEDIITIFKY LTDKDAFETH YRRLFAKRLI HGTSTSAEDE
510 520 530 540 550
ENIIQRLQAA NSMEYTGKIT KMFQDIRLSK ILEDDFAVAL KNEPDYSKAK
560 570 580 590 600
YPDLQPFVLA ENMWPFSYQE VEFKLPKELV PSHEKLKESY SQKHNGRILK
610 620 630 640 650
WLWPLCRGEL KADIGKPGRM PFNFTVTLFQ MAILLLYNDA DVLTLENIQE
660 670 680 690 700
GTSLTIQHIA AAMVPFIKFK LIQQVPPGLD ALVKPETQFK LSRPYKALKT
710 720 730 740 750
NINFASGVKN DILQSLSGGG HDNHGNKLGN KRLTEDERIE KELNTERQIF
760 770 780 790 800
LEACIVRIMK AKRNLPHTTL VNECIAQSHQ RFNAKVSMVK RAIDSLIQKG
810
YLQRGDDGES YAYLA
Length:815
Mass (Da):93,944
Last modified:November 1, 1997 - v1
Checksum:i22BC8B35034EDDEF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43564 Genomic DNA Translation: AAB38821.1
X96876 Genomic DNA Translation: CAA65628.1
Z74180 Genomic DNA Translation: CAA98702.1
BK006938 Genomic DNA Translation: DAA11727.1
PIRiS67675
RefSeqiNP_010150.1, NM_001180191.1

Genome annotation databases

EnsemblFungiiYDL132W; YDL132W; YDL132W
GeneIDi851424
KEGGisce:YDL132W

Similar proteinsi

Entry informationi

Entry nameiCDC53_YEAST
AccessioniPrimary (citable) accession number: Q12018
Secondary accession number(s): D6VRL7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 25, 2018
This is version 149 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