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P53197 (CDH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
APC/C activator protein CDH1
Alternative name(s):
CDC20 homolog 1
Homolog of CDC twenty 1
Gene names
Name:CDH1
Synonyms:HCT1
Ordered Locus Names:YGL003C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.9

Subunit structure

Associates with the APC/C complex. Interacts with CLB2, CLB3, CDC5, HSL1, MSN5 and PSE1. Ref.7 Ref.8 Ref.10

Subcellular location

Cytoplasm. Nucleus. Note: Nuclear import and export are mediated by the importin PSE1 and the exportin MSN5. Ref.10

Domain

The C-box is required for the association with the APC/C complex By similarity. Ref.7

Post-translational modification

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. Ref.4 Ref.5 Ref.11

Sequence similarities

Belongs to the WD repeat CDC20/Fizzy family.

Contains 7 WD repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACM1Q089818EBI-23684,EBI-2345174

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 566566APC/C activator protein CDH1
PRO_0000050904

Regions

Repeat258 – 29841WD 1
Repeat300 – 33940WD 2
Repeat342 – 37938WD 3
Repeat383 – 42240WD 4
Repeat425 – 46743WD 5
Repeat469 – 51042WD 6
Repeat513 – 55240WD 7
Motif55 – 617C-box
Compositional bias32 – 387Poly-Ser

Amino acid modifications

Modified residue2131Phosphoserine Ref.13

Experimental info

Mutagenesis121T → A: Abolishes phosphorylation; when associated with A-16; A-42; A-157; A-169; A-173; A-176; A-227 and A-239. Ref.4
Mutagenesis161S → A: Abolishes phosphorylation; when associated with A-12; A-42; A-157; A-169; A-173; A-176; A-227 and A-239. Ref.4
Mutagenesis421S → A: Abolishes phosphorylation; when associated with A-12; A-16; A-157; A-169; A-173; A-176; A-227 and A-239. Ref.4
Mutagenesis1571T → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-169; A-173; A-176; A-227 and A-239. Ref.4
Mutagenesis1691S → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-173; A-176; A-227 and A-239. Ref.4
Mutagenesis1731T → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-169; A-176; A-227 and A-239. Ref.4
Mutagenesis1761T → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-169; A-173; A-227 and A-239. Ref.4
Mutagenesis2271S → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-169; A-173; A-176 and A-239. Ref.4
Mutagenesis2391S → A: Abolishes phosphorylation; when associated with A-12; A-16; A-42; A-157; A-169; A-173; A-176 and A-227. Ref.4

Secondary structure

...................................................................... 566
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53197 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: DA6DE5545607906B

FASTA56662,821
        10         20         30         40         50         60 
MSTNLNPFMN NTPSSSPLKG SESKRVSKRP ISSSSSASLL SSPSRRSRPS TVYGDRYIPS 

        70         80         90        100        110        120 
RTDIDFNSIV SISSMASVPA LNPSSTEDQV EYQKERQAHE TYNTLLKNEL FGEMLSKDTV 

       130        140        150        160        170        180 
GSESSIDRIK NTRPSTRGNV HAENTTRHGY ELERVSTPPP EAAGLEEFSP HSTPVTPRRL 

       190        200        210        220        230        240 
FTSQQDEITR PSSNSVRGAS LLTYQQRKGR RLSAASLLQS QFFDSMSPVR PDSKQLLLSP 

       250        260        270        280        290        300 
GKQFRQIAKV PYRVLDAPSL ADDFYYSLID WSSTDVLAVA LGKSIFLTDN NTGDVVHLCD 

       310        320        330        340        350        360 
TENEYTSLSW IGAGSHLAVG QANGLVEIYD VMKRKCIRTL SGHIDRVACL SWNNHVLTSG 

       370        380        390        400        410        420 
SRDHRILHRD VRMPDPFFET IESHTQEVCG LKWNVADNKL ASGGNDNVVH VYEGTSKSPI 

       430        440        450        460        470        480 
LTFDEHKAAV KAMAWSPHKR GVLATGGGTA DRRLKIWNVN TSIKMSDIDS GSQICNMVWS 

       490        500        510        520        530        540 
KNTNELVTSH GYSKYNLTLW DCNSMDPIAI LKGHSFRVLH LTLSNDGTTV VSGAGDETLR 

       550        560 
YWKLFDKPKA KVQPNSLIFD AFNQIR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Targets of the cyclin-dependent kinase Cdk1."
Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K., Shokat K.M., Morgan D.O.
Nature 425:859-864(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z72525 Genomic DNA. Translation: CAA96703.1.
AY693078 Genomic DNA. Translation: AAT93097.1.
BK006941 Genomic DNA. Translation: DAA08096.1.
PIRS64005.
RefSeqNP_011512.1. NM_001180868.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BH6X-ray2.90A/B/C/D/E/F/G/H241-548[»]
ProteinModelPortalP53197.
SMRP53197. Positions 244-548.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33242. 273 interactions.
DIPDIP-5915N.
IntActP53197. 4 interactions.
MINTMINT-673168.
STRING4932.YGL003C.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL003C; YGL003C; YGL003C.
GeneID852881.
KEGGsce:YGL003C.

Organism-specific databases

CYGDYGL003c.
SGDS000002971. CDH1.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00750000117562.
HOGENOMHOG000195514.
KOK03364.
OMALKWNVEE.
OrthoDBEOG7MSMZF.

Enzyme and pathway databases

BioCycYEAST:G3O-30527-MONOMER.

Gene expression databases

GenevestigatorP53197.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 4 hits.
[Graphical view]
SMARTSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972526.
PROP53197.

Entry information

Entry nameCDH1_YEAST
AccessionPrimary (citable) accession number: P53197
Secondary accession number(s): D6VUD5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references