P38042 (CDC27_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Anaphase-promoting complex subunit CDC27

Alternative name(s):
Anaphase-promoting complex subunit 3
Cell division control protein 27

Gene names

Name:	CDC27
Synonyms:	APC3, SNB1
Ordered Locus Names:	YBL084C
ORF Names:	YBL0718

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	758 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. Ref.5 Ref.6 Ref.7
Pathway	Protein modification; protein ubiquitination.
Subunit structure	The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. Ref.5 Ref.7
Subcellular location	Cytoplasm. Nucleus Ref.8.
Post-translational modification	Phosphorylated by CDC28, which is required for the early mitotic activity of the APC/C in its CDC20-bound form. Ref.6 Ref.10
Miscellaneous	Present with 593 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the APC3/CDC27 family. Contains 8 TPR repeats.
Sequence caution	The sequence CAA56022.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Domain	Repeat TPR repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay. Source: SGD cell division Inferred from electronic annotation. Source: UniProtKB-KW cyclin catabolic process Traceable author statement. Source: SGD mitotic metaphase/anaphase transition Traceable author statement. Source: SGD mitotic sister chromatid segregation Traceable author statement. Source: SGD mitotic spindle elongation Traceable author statement. Source: SGD
Cellular component	anaphase-promoting complex Inferred from direct assay. Source: SGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	binding Inferred from electronic annotation. Source: InterPro ubiquitin-protein ligase activity Traceable author statement. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 758	758	Anaphase-promoting complex subunit CDC27		PRO_0000106274
Regions
	Repeat	154 – 187	34	TPR 1
	Repeat	472 – 505	34	TPR 2
	Repeat	540 – 573	34	TPR 3
	Repeat	574 – 607	34	TPR 4
	Repeat	608 – 641	34	TPR 5
	Repeat	642 – 675	34	TPR 6
	Repeat	676 – 709	34	TPR 7
	Repeat	710 – 743	34	TPR 8
	Compositional bias	365 – 388	24	Poly-Asn
Amino acid modifications
	Modified residue	354	1	Phosphoserine Ref.10
Experimental info
	Mutagenesis	267	1	S → A: Abolishes phosphorylation; when associated with A-304; A-328; A-351 and A-397. Ref.6
	Mutagenesis	304	1	T → A: Abolishes phosphorylation; when associated with A-267; A-304; A-351 and A-397. Ref.6
	Mutagenesis	328	1	S → A: Abolishes phosphorylation; when associated with A-267; A-304; A-328 and A-397. Ref.6
	Mutagenesis	351	1	T → A: Abolishes phosphorylation; when associated with A-267; A-304; A-328 and A-304. Ref.6
	Mutagenesis	397	1	T → A: Abolishes phosphorylation; when associated with A-304; A-328; A-351 and A-397. Ref.6
	Mutagenesis	613	1	G → D in CDC27-633; G2/M cell cycle arrest at 35 degrees Celsius. Ref.4
	Mutagenesis	614	1	L → GL: Abolishes interaction with CDC23. Ref.5
	Sequence conflict	430	1	S → Q in CAA56022. Ref.1
	Sequence conflict	430	1	S → Q in CAA84905. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P38042 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: A1ECA067AF8784E3	FASTA	758	85,396
	10 20 30 40 50 60 MAVNPELAPF TLSRGIPSFD DQALSTIIQL QDCIQQAIQQ LNYSTAEFLA ELLYAECSIL 70 80 90 100 110 120 DKSSVYWSDA VYLYALSLFL NKSYHTAFQI SKEFKEYHLG IAYIFGRCAL QLSQGVNEAI 130 140 150 160 170 180 LTLLSIINVF SSNSSNTRIN MVLNSNLVHI PDLATLNCLL GNLYMKLDHS KEGAFYHSEA 190 200 210 220 230 240 LAINPYLWES YEAICKMRAT VDLKRVFFDI AGKKSNSHNN NAASSFPSTS LSHFEPRSQP 250 260 270 280 290 300 SLYSKTNKNG NNNINNNVNT LFQSSNSPPS TSASSFSSIQ HFSRSQQQQA NTSIRTCQNK 310 320 330 340 350 360 NTQTPKNPAI NSKTSSALPN NISMNLVSPS SKQPTISSLA KVYNRNKLLT TPPSKLLNND 370 380 390 400 410 420 RNHQNNNNNN NNNNNNNNNN NNNNNNNNII NKTTFKTPRN LYSSTGRLTT SKKNPRSLII 430 440 450 460 470 480 SNSILTSDYS ITLPEIMYNF ALILRSSSQY NSFKAIRLFE SQIPSHIKDT MPWCLVQLGK 490 500 510 520 530 540 LHFEIINYDM SLKYFNRLKD LQPARVKDME IFSTLLWHLH DKVKSSNLAN GLMDTMPNKP 550 560 570 580 590 600 ETWCCIGNLL SLQKDHDAAI KAFEKATQLD PNFAYAYTLQ GHEHSSNDSS DSAKTCYRKA 610 620 630 640 650 660 LACDPQHYNA YYGLGTSAMK LGQYEEALLY FEKARSINPV NVVLICCCGG SLEKLGYKEK 670 680 690 700 710 720 ALQYYELACH LQPTSSLSKY KMGQLLYSMT RYNVALQTFE ELVKLVPDDA TAHYLLGQTY 730 740 750 RIVGRKKDAI KELTVAMNLD PKGNQVIIDE LQKCHMQE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II." Obermaier B., Gassenhuber J., Piravandi E., Domdey H. Yeast 11:1103-1112(1995) [PubMed: 7502586] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 430. Strain: ATCC 204508 / S288c.
[4]	"TPR proteins as essential components of the yeast cell cycle." Sikorski R.S., Michaud W.A., Wootton J.C., Boguski M.S., Connelly C., Hieter P.A. Cold Spring Harb. Symp. Quant. Biol. 56:663-673(1991) [PubMed: 1819514] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE, MUTAGENESIS OF GLY-613.
[5]	"Cdc16p, Cdc23p and Cdc27p form a complex essential for mitosis." Lamb J.R., Michaud W.A., Sikorski R.S., Hieter P.A. EMBO J. 13:4321-4328(1994) [PubMed: 7925276] [Abstract] Cited for: FUNCTION, SUBUNIT, DOMAINS TPR REPEATS, MUTAGENESIS OF LEU-614.
[6]	"Phosphorylation by Cdc28 activates the Cdc20-dependent activity of the anaphase-promoting complex." Rudner A.D., Murray A.W. J. Cell Biol. 149:1377-1390(2000) [PubMed: 10871279] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION BY CDC28, MUTAGENESIS OF SER-267; THR-304; SER-328; THR-351 AND THR-397.
[7]	"Swm1/Apc13 is an evolutionarily conserved subunit of the anaphase-promoting complex stabilizing the association of Cdc16 and Cdc27." Schwickart M., Havlis J., Habermann B., Bogdanova A., Camasses A., Oelschlaegel T., Shevchenko A., Zachariae W. Mol. Cell. Biol. 24:3562-3576(2004) [PubMed: 15060174] [Abstract] Cited for: FUNCTION, SUBUNIT.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X79489 Genomic DNA. Translation: CAA56022.1. Different initiation. Z35845 Genomic DNA. Translation: CAA84905.1. BK006936 Genomic DNA. Translation: DAA07040.2.
PIR	S45825.
RefSeq	NP_009469.2. NM_001178324.2.
3D structure databases
ProteinModelPortal	P38042.
SMR	P38042. Positions 435-747.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-796N.
IntAct	P38042. 40 interactions.
MINT	MINT-652602.
STRING	P38042.
Proteomic databases
PeptideAtlas	P38042.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	852194.
KEGG	sce:YBL084C.
NMPDR	fig|4932.3.peg.155.
Organism-specific databases
CYGD	YBL084c.
SGD	S000000180. CDC27.
Phylogenomic databases
eggNOG	fuNOG06767.
GeneTree	EFGT00050000000806.
HOGENOM	HBG397840.
OMA	HHFRMAF.
OrthoDB	EOG4G1QQV.
Gene expression databases
ArrayExpress	P38042.
Genevestigator	P38042.
GermOnline	YBL084C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001440. TPR-1. IPR013026. TPR-contain. IPR011990. TPR-like_helical. IPR019734. TPR_repeat. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 4 hits.
KO	K03350.
Pfam	PF00515. TPR_1. 2 hits. [Graphical view]
SMART	SM00028. TPR. 8 hits. [Graphical view]
PROSITE	PS50005. TPR. 8 hits. PS50293. TPR_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	970679.

Entry information

Entry name

CDC27_YEAST

Accession

Primary (citable) accession number: P38042
Secondary accession number(s): D6VPS0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	July 27, 2011
Last modified:	December 14, 2011
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program