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P53197

- CDH1_YEAST

UniProt

P53197 - CDH1_YEAST

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Protein
APC/C activator protein CDH1
Gene
CDH1, HCT1, YGL003C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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. protein binding Source: IntAct
  4. ubiquitin-protein transferase activator activity Source: SGD

GO - Biological processi

  1. activation of mitotic anaphase-promoting complex activity Source: SGD
  2. mitotic nuclear division Source: UniProtKB-KW
  3. negative regulation of spindle pole body separation Source: SGD
  4. positive regulation of cyclin catabolic process Source: SGD
  5. positive regulation of mitotic metaphase/anaphase transition Source: SGD
  6. 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_188466. 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: Chromosome VII

Organism-specific databases

CYGDiYGL003c.
SGDiS000002971. CDH1.

Subcellular locationi

Cytoplasm. Nucleus
Note: Nuclear import and export are mediated by the importin PSE1 and the exportin MSN5.1 Publication

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 CDH1
PRO_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.3 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. 273 interactions.
DIPiDIP-5915N.
IntActiP53197. 4 interactions.
MINTiMINT-673168.
STRINGi4932.YGL003C.

Structurei

Secondary structure

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

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 7 WD repeats.

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00750000117562.
HOGENOMiHOG000195514.
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

MSTNLNPFMN NTPSSSPLKG SESKRVSKRP ISSSSSASLL SSPSRRSRPS    50
TVYGDRYIPS RTDIDFNSIV SISSMASVPA LNPSSTEDQV EYQKERQAHE 100
TYNTLLKNEL FGEMLSKDTV GSESSIDRIK NTRPSTRGNV HAENTTRHGY 150
ELERVSTPPP EAAGLEEFSP HSTPVTPRRL FTSQQDEITR PSSNSVRGAS 200
LLTYQQRKGR RLSAASLLQS QFFDSMSPVR PDSKQLLLSP GKQFRQIAKV 250
PYRVLDAPSL ADDFYYSLID WSSTDVLAVA LGKSIFLTDN NTGDVVHLCD 300
TENEYTSLSW IGAGSHLAVG QANGLVEIYD VMKRKCIRTL SGHIDRVACL 350
SWNNHVLTSG SRDHRILHRD VRMPDPFFET IESHTQEVCG LKWNVADNKL 400
ASGGNDNVVH VYEGTSKSPI LTFDEHKAAV KAMAWSPHKR GVLATGGGTA 450
DRRLKIWNVN TSIKMSDIDS GSQICNMVWS KNTNELVTSH GYSKYNLTLW 500
DCNSMDPIAI LKGHSFRVLH LTLSNDGTTV VSGAGDETLR YWKLFDKPKA 550
KVQPNSLIFD AFNQIR 566
Length:566
Mass (Da):62,821
Last modified:October 1, 1996 - v1
Checksum:iDA6DE5545607906B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
Z72525 Genomic DNA. Translation: CAA96703.1 .
AY693078 Genomic DNA. Translation: AAT93097.1 .
BK006941 Genomic DNA. Translation: DAA08096.1 .
PIRi S64005.
RefSeqi NP_011512.1. NM_001180868.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BH6 X-ray 2.90 A/B/C/D/E/F/G/H 241-548 [» ]
ProteinModelPortali P53197.
SMRi P53197. Positions 244-548.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33242. 273 interactions.
DIPi DIP-5915N.
IntActi P53197. 4 interactions.
MINTi MINT-673168.
STRINGi 4932.YGL003C.

Proteomic databases

MaxQBi P53197.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL003C ; YGL003C ; YGL003C .
GeneIDi 852881.
KEGGi sce:YGL003C.

Organism-specific databases

CYGDi YGL003c.
SGDi S000002971. CDH1.

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00750000117562.
HOGENOMi HOG000195514.
KOi K03364.
OMAi LKWNVEE.
OrthoDBi EOG7MSMZF.

Enzyme and pathway databases

BioCyci YEAST:G3O-30527-MONOMER.
Reactomei REACT_188466. Regulation of APC/C activators between G1/S and early anaphase.

Miscellaneous databases

NextBioi 972526.
PROi P53197.

Gene expression databases

Genevestigatori P53197.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF00400. WD40. 4 hits.
[Graphical view ]
SMARTi SM00320. WD40. 5 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
PROSITEi PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 126 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

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