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Protein

APC/C activator protein CDH1

Gene

CDH1

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

Activator protein that regulates the ubiquitin ligase activity and substrate specificity of the anaphase promoting complex/cyclosome (APC/C). During telophase and in the subsequent G1 phase of the cell cycle, recognizes and binds proteins containing a destruction box (D-box) and an additional degradation signal termed the KEN box including ASE1, CDC20, the B-type cyclins CLB2 and CLB3, the polo-like kinase CDC5 and HSL1, and recruits them in a C-box-dependent manner to the APC/C for ubiquitination and subsequent proteolysis. Required for exit from mitosis, cytokinesis and formation of prereplicative complexes in G1. Probably is the target of a BUB2-dependent spindle checkpoint pathway.3 Publications

GO - Molecular functioni

  • anaphase-promoting complex binding Source: SGD
  • cyclin binding Source: SGD
  • ubiquitin-protein transferase activator activity Source: SGD

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of mitotic spindle assembly checkpoint Source: SGD
  • negative regulation of spindle pole body separation Source: SGD
  • positive regulation of cellular protein catabolic process Source: SGD
  • positive regulation of mitotic metaphase/anaphase transition Source: SGD
  • positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: SGD
  • positive regulation of ubiquitin protein ligase activity Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

BioCyciYEAST:G3O-30527-MONOMER.
ReactomeiR-SCE-141405. Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
R-SCE-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-SCE-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-SCE-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-SCE-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-SCE-5689880. Ub-specific processing proteases.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-69656. Cyclin A:Cdk2-associated events at S phase entry.

Names & Taxonomyi

Protein namesi
Recommended name:
APC/C activator protein CDH1
Alternative name(s):
CDC20 homolog 1
Homolog of CDC twenty 1
Gene namesi
Name:CDH1
Synonyms:HCT1
Ordered Locus Names:YGL003C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL003C.
SGDiS000002971. CDH1.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

  • Note: Nuclear import and export are mediated by the importin PSE1 and the exportin MSN5.

GO - Cellular componenti

  • anaphase-promoting complex Source: SGD
  • cytoplasm Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi12T → A: Abolishes phosphorylation; when associated with A-16; A-42; A-157; A-169; A-173; A-176; A-227 and A-239. 1 Publication1
Mutagenesisi16S → A: Abolishes phosphorylation; when associated with A-12; A-42; A-157; A-169; A-173; A-176; A-227 and A-239. 1 Publication1
Mutagenesisi42S → A: Abolishes phosphorylation; when associated with A-12; A-16; A-157; A-169; A-173; A-176; A-227 and A-239. 1 Publication1
Mutagenesisi157T → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-169; A-173; A-176; A-227 and A-239. 1 Publication1
Mutagenesisi169S → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-173; A-176; A-227 and A-239. 1 Publication1
Mutagenesisi173T → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-169; A-176; A-227 and A-239. 1 Publication1
Mutagenesisi176T → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-169; A-173; A-227 and A-239. 1 Publication1
Mutagenesisi227S → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-169; A-173; A-176 and A-239. 1 Publication1
Mutagenesisi239S → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-169; A-173; A-176 and A-227. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000509041 – 566APC/C activator protein CDH1Add BLAST566

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei213PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated at multiple sites by CDC28, probably in its CLB5 bound form, in S, G2 and M phase of the cell cycle, thereby blocking the association of CDH1 to the APC/C and promoting nuclear export of CDH1 by MSN5. Dephosphorylated and activated by CDC14 in late anaphase, which may be necessary for PSE1-dependent nuclear localization.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53197.
PRIDEiP53197.

PTM databases

iPTMnetiP53197.

Interactioni

Subunit structurei

Associates with the APC/C complex. Interacts with CLB2, CLB3, CDC5, HSL1, MSN5 and PSE1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACM1Q089818EBI-23684,EBI-2345174

GO - Molecular functioni

  • anaphase-promoting complex binding Source: SGD
  • cyclin binding Source: SGD

Protein-protein interaction databases

BioGridi33242. 274 interactors.
DIPiDIP-5915N.
IntActiP53197. 4 interactors.
MINTiMINT-673168.

Structurei

Secondary structure

1566
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi252 – 256Combined sources5
Beta strandi269 – 271Combined sources3
Beta strandi275 – 281Combined sources7
Beta strandi284 – 289Combined sources6
Turni290 – 292Combined sources3
Beta strandi295 – 300Combined sources6
Beta strandi305 – 310Combined sources6
Beta strandi314 – 321Combined sources8
Beta strandi326 – 330Combined sources5
Turni331 – 334Combined sources4
Beta strandi335 – 340Combined sources6
Beta strandi347 – 353Combined sources7
Beta strandi356 – 364Combined sources9
Beta strandi366 – 370Combined sources5
Beta strandi373 – 376Combined sources4
Beta strandi378 – 381Combined sources4
Beta strandi388 – 393Combined sources6
Beta strandi395 – 397Combined sources3
Beta strandi399 – 404Combined sources6
Beta strandi409 – 413Combined sources5
Beta strandi420 – 423Combined sources4
Beta strandi430 – 435Combined sources6
Beta strandi437 – 439Combined sources3
Beta strandi442 – 447Combined sources6
Turni449 – 451Combined sources3
Beta strandi453 – 458Combined sources6
Turni459 – 462Combined sources4
Beta strandi463 – 469Combined sources7
Beta strandi474 – 479Combined sources6
Beta strandi481 – 484Combined sources4
Beta strandi486 – 490Combined sources5
Beta strandi497 – 500Combined sources4
Beta strandi502 – 504Combined sources3
Beta strandi507 – 511Combined sources5
Beta strandi518 – 523Combined sources6
Beta strandi527 – 534Combined sources8
Turni535 – 537Combined sources3
Beta strandi538 – 543Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BH6X-ray2.90A/B/C/D/E/F/G/H241-548[»]
5A31electron microscopy4.30R102-546[»]
ProteinModelPortaliP53197.
SMRiP53197.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati258 – 298WD 1Add BLAST41
Repeati300 – 339WD 2Add BLAST40
Repeati342 – 379WD 3Add BLAST38
Repeati383 – 422WD 4Add BLAST40
Repeati425 – 467WD 5Add BLAST43
Repeati469 – 510WD 6Add BLAST42
Repeati513 – 552WD 7Add BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi55 – 61C-box7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi32 – 38Poly-Ser7

Domaini

The C-box is required for the association with the APC/C complex.By similarity

Sequence similaritiesi

Belongs to the WD repeat CDC20/Fizzy family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

GeneTreeiENSGT00860000133834.
HOGENOMiHOG000195514.
InParanoidiP53197.
KOiK03364.
OMAiLKWNVEE.
OrthoDBiEOG092C2B79.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR024977. Apc4_WD40_dom.
IPR033010. Cdc20/Fizzy.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR19918. PTHR19918. 2 hits.
PfamiPF12894. ANAPC4_WD40. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53197-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTNLNPFMN NTPSSSPLKG SESKRVSKRP ISSSSSASLL SSPSRRSRPS
60 70 80 90 100
TVYGDRYIPS RTDIDFNSIV SISSMASVPA LNPSSTEDQV EYQKERQAHE
110 120 130 140 150
TYNTLLKNEL FGEMLSKDTV GSESSIDRIK NTRPSTRGNV HAENTTRHGY
160 170 180 190 200
ELERVSTPPP EAAGLEEFSP HSTPVTPRRL FTSQQDEITR PSSNSVRGAS
210 220 230 240 250
LLTYQQRKGR RLSAASLLQS QFFDSMSPVR PDSKQLLLSP GKQFRQIAKV
260 270 280 290 300
PYRVLDAPSL ADDFYYSLID WSSTDVLAVA LGKSIFLTDN NTGDVVHLCD
310 320 330 340 350
TENEYTSLSW IGAGSHLAVG QANGLVEIYD VMKRKCIRTL SGHIDRVACL
360 370 380 390 400
SWNNHVLTSG SRDHRILHRD VRMPDPFFET IESHTQEVCG LKWNVADNKL
410 420 430 440 450
ASGGNDNVVH VYEGTSKSPI LTFDEHKAAV KAMAWSPHKR GVLATGGGTA
460 470 480 490 500
DRRLKIWNVN TSIKMSDIDS GSQICNMVWS KNTNELVTSH GYSKYNLTLW
510 520 530 540 550
DCNSMDPIAI LKGHSFRVLH LTLSNDGTTV VSGAGDETLR YWKLFDKPKA
560
KVQPNSLIFD AFNQIR
Length:566
Mass (Da):62,821
Last modified:October 1, 1996 - v1
Checksum:iDA6DE5545607906B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72525 Genomic DNA. Translation: CAA96703.1.
AY693078 Genomic DNA. Translation: AAT93097.1.
BK006941 Genomic DNA. Translation: DAA08096.1.
PIRiS64005.
RefSeqiNP_011512.1. NM_001180868.1.

Genome annotation databases

EnsemblFungiiYGL003C; YGL003C; YGL003C.
GeneIDi852881.
KEGGisce:YGL003C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72525 Genomic DNA. Translation: CAA96703.1.
AY693078 Genomic DNA. Translation: AAT93097.1.
BK006941 Genomic DNA. Translation: DAA08096.1.
PIRiS64005.
RefSeqiNP_011512.1. NM_001180868.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BH6X-ray2.90A/B/C/D/E/F/G/H241-548[»]
5A31electron microscopy4.30R102-546[»]
ProteinModelPortaliP53197.
SMRiP53197.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33242. 274 interactors.
DIPiDIP-5915N.
IntActiP53197. 4 interactors.
MINTiMINT-673168.

PTM databases

iPTMnetiP53197.

Proteomic databases

MaxQBiP53197.
PRIDEiP53197.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL003C; YGL003C; YGL003C.
GeneIDi852881.
KEGGisce:YGL003C.

Organism-specific databases

EuPathDBiFungiDB:YGL003C.
SGDiS000002971. CDH1.

Phylogenomic databases

GeneTreeiENSGT00860000133834.
HOGENOMiHOG000195514.
InParanoidiP53197.
KOiK03364.
OMAiLKWNVEE.
OrthoDBiEOG092C2B79.

Enzyme and pathway databases

BioCyciYEAST:G3O-30527-MONOMER.
ReactomeiR-SCE-141405. Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
R-SCE-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-SCE-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-SCE-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-SCE-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-SCE-5689880. Ub-specific processing proteases.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-69656. Cyclin A:Cdk2-associated events at S phase entry.

Miscellaneous databases

PROiP53197.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR024977. Apc4_WD40_dom.
IPR033010. Cdc20/Fizzy.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR19918. PTHR19918. 2 hits.
PfamiPF12894. ANAPC4_WD40. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCDH1_YEAST
AccessioniPrimary (citable) accession number: P53197
Secondary accession number(s): D6VUD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.