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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

  1. anaphase-promoting complex binding Source: SGD
  2. cyclin binding Source: SGD
  3. ubiquitin-protein transferase activator activity Source: SGD

GO - Biological processi

  1. activation of APC-Cdc20 complex activity Source: SGD
  2. cell division Source: UniProtKB-KW
  3. mitotic nuclear division Source: UniProtKB-KW
  4. negative regulation of spindle pole body separation Source: SGD
  5. positive regulation of cyclin catabolic process Source: SGD
  6. positive regulation of mitotic metaphase/anaphase transition Source: SGD
  7. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

BioCyciYEAST:G3O-30527-MONOMER.
ReactomeiREACT_280552. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_292147. Regulation of APC/C activators between G1/S and early anaphase.

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
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL003c.
EuPathDBiFungiDB:YGL003C.
SGDiS000002971. CDH1.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Nucleus 1 Publication

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

GO - Cellular componenti

  1. anaphase-promoting complex Source: SGD
  2. cytoplasm Source: SGD
  3. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121T → A: Abolishes phosphorylation; when associated with A-16; A-42; A-157; A-169; A-173; A-176; A-227 and A-239. 1 Publication
Mutagenesisi16 – 161S → A: Abolishes phosphorylation; when associated with A-12; A-42; A-157; A-169; A-173; A-176; A-227 and A-239. 1 Publication
Mutagenesisi42 – 421S → A: Abolishes phosphorylation; when associated with A-12; A-16; A-157; A-169; A-173; A-176; A-227 and A-239. 1 Publication
Mutagenesisi157 – 1571T → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-169; A-173; A-176; A-227 and A-239. 1 Publication
Mutagenesisi169 – 1691S → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-173; A-176; A-227 and A-239. 1 Publication
Mutagenesisi173 – 1731T → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-169; A-176; A-227 and A-239. 1 Publication
Mutagenesisi176 – 1761T → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-169; A-173; A-227 and A-239. 1 Publication
Mutagenesisi227 – 2271S → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-169; A-173; A-176 and A-239. 1 Publication
Mutagenesisi239 – 2391S → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-169; A-173; A-176 and A-227. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 566566APC/C activator protein CDH1PRO_0000050904Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei213 – 2131Phosphoserine1 Publication

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.

Expressioni

Gene expression databases

GenevestigatoriP53197.

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

Protein-protein interaction databases

BioGridi33242. 271 interactions.
DIPiDIP-5915N.
IntActiP53197. 4 interactions.
MINTiMINT-673168.
STRINGi4932.YGL003C.

Structurei

Secondary structure

1
566
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi252 – 2565Combined sources
Beta strandi269 – 2713Combined sources
Beta strandi275 – 2817Combined sources
Beta strandi284 – 2896Combined sources
Turni290 – 2923Combined sources
Beta strandi295 – 3006Combined sources
Beta strandi305 – 3106Combined sources
Beta strandi314 – 3218Combined sources
Beta strandi326 – 3305Combined sources
Turni331 – 3344Combined sources
Beta strandi335 – 3406Combined sources
Beta strandi347 – 3537Combined sources
Beta strandi356 – 3649Combined sources
Beta strandi366 – 3705Combined sources
Beta strandi373 – 3764Combined sources
Beta strandi378 – 3814Combined sources
Beta strandi388 – 3936Combined sources
Beta strandi395 – 3973Combined sources
Beta strandi399 – 4046Combined sources
Beta strandi409 – 4135Combined sources
Beta strandi420 – 4234Combined sources
Beta strandi430 – 4356Combined sources
Beta strandi437 – 4393Combined sources
Beta strandi442 – 4476Combined sources
Turni449 – 4513Combined sources
Beta strandi453 – 4586Combined sources
Turni459 – 4624Combined sources
Beta strandi463 – 4697Combined sources
Beta strandi474 – 4796Combined sources
Beta strandi481 – 4844Combined sources
Beta strandi486 – 4905Combined sources
Beta strandi497 – 5004Combined sources
Beta strandi502 – 5043Combined sources
Beta strandi507 – 5115Combined sources
Beta strandi518 – 5236Combined sources
Beta strandi527 – 5348Combined sources
Turni535 – 5373Combined sources
Beta strandi538 – 5436Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BH6X-ray2.90A/B/C/D/E/F/G/H241-548[»]
ProteinModelPortaliP53197.
SMRiP53197. Positions 244-548.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati258 – 29841WD 1Add
BLAST
Repeati300 – 33940WD 2Add
BLAST
Repeati342 – 37938WD 3Add
BLAST
Repeati383 – 42240WD 4Add
BLAST
Repeati425 – 46743WD 5Add
BLAST
Repeati469 – 51042WD 6Add
BLAST
Repeati513 – 55240WD 7Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi55 – 617C-box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi32 – 387Poly-Ser

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

eggNOGiCOG2319.
GeneTreeiENSGT00760000119369.
HOGENOMiHOG000195514.
InParanoidiP53197.
KOiK03364.
OMAiLKWNVEE.
OrthoDBiEOG7MSMZF.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 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
EntryMethodResolution (Å)ChainPositionsPDBsum
4BH6X-ray2.90A/B/C/D/E/F/G/H241-548[»]
ProteinModelPortaliP53197.
SMRiP53197. Positions 244-548.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33242. 271 interactions.
DIPiDIP-5915N.
IntActiP53197. 4 interactions.
MINTiMINT-673168.
STRINGi4932.YGL003C.

Proteomic databases

MaxQBiP53197.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYGL003c.
EuPathDBiFungiDB:YGL003C.
SGDiS000002971. CDH1.

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000119369.
HOGENOMiHOG000195514.
InParanoidiP53197.
KOiK03364.
OMAiLKWNVEE.
OrthoDBiEOG7MSMZF.

Enzyme and pathway databases

BioCyciYEAST:G3O-30527-MONOMER.
ReactomeiREACT_280552. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_292147. Regulation of APC/C activators between G1/S and early anaphase.

Miscellaneous databases

NextBioi972526.
PROiP53197.

Gene expression databases

GenevestigatoriP53197.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 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...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Control of cyclin ubiquitination by CDK-regulated binding of Hct1 to the anaphase promoting complex."
    Zachariae W., Schwab M., Nasmyth K., Seufert W.
    Science 282:1721-1724(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH THE APC/C COMPLEX, PHOSPHORYLATION BY CDC28, MUTAGENESIS OF THR-12; SER-16; SER-42; THR-157; SER-169; THR-173; THR-176; SER-227 AND SER-239.
  5. "Inhibitory phosphorylation of the APC regulator Hct1 is controlled by the kinase Cdc28 and the phosphatase Cdc14."
    Jaspersen S.L., Charles J.F., Morgan D.O.
    Curr. Biol. 9:227-236(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEPHOSPHORYLATION BY CDC14.
  6. "Sister chromatid separation and chromosome re-duplication are regulated by different mechanisms in response to spindle damage."
    Alexandru G., Zachariae W., Schleiffer A., Nasmyth K.
    EMBO J. 18:2707-2721(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS SPINDLE CHECKPOINT TARGET.
  7. "Yeast Hct1 recognizes the mitotic cyclin Clb2 and other substrates of the ubiquitin ligase APC."
    Schwab M., Neutzner M., Moecker D., Seufert W.
    EMBO J. 20:5165-5175(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CLB2; CLB3 AND CDC5, DOMAIN C-BOX MOTIF.
  8. "D box and KEN box motifs in budding yeast Hsl1p are required for APC-mediated degradation and direct binding to Cdc20p and Cdh1p."
    Burton J.L., Solomon M.J.
    Genes Dev. 15:2381-2395(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSL1.
  9. "Activity of the APC(Cdh1) form of the anaphase-promoting complex persists until S phase and prevents the premature expression of Cdc20p."
    Huang J.N., Park I., Ellingson E., Littlepage L.E., Pellman D.
    J. Cell Biol. 154:85-94(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ASE1 AND CDC20 DEGRADATION.
  10. "Cell cycle-dependent nuclear export of Cdh1p may contribute to the inactivation of APC/C(Cdh1)."
    Jaquenoud M., van Drogen F., Peter M.
    EMBO J. 21:6515-6526(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MSN5 AND PSE1.
  11. Cited for: PHOSPHORYLATION BY CDC28.
  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: 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: April 29, 2015
This is version 134 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

External Data

Dasty 3

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 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.