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Protein

Anaphase-promoting complex subunit CDC16

Gene

CDC16

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

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.5 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Biological processi

  • anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: SGD
  • cell division Source: UniProtKB-KW
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of DNA-dependent DNA replication initiation Source: SGD
  • protein ubiquitination Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-31830-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit CDC16
Alternative name(s):
Cell division control protein 16
Gene namesi
Name:CDC16
Ordered Locus Names:YKL022C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL022C.
SGDiS000001505. CDC16.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441S → A: Abolishes phosphorylation; when associated with A-59; A-95; A-103; A-115 and A-406. 1 Publication
Mutagenesisi59 – 591S → A: Abolishes phosphorylation; when associated with A-44; A-95; A-103; A-115 and A-406. 1 Publication
Mutagenesisi95 – 951S → A: Abolishes phosphorylation; when associated with A-44; A-59; A-103; A-115 and A-406. 1 Publication
Mutagenesisi103 – 1031S → A: Abolishes phosphorylation; when associated with A-44; A-59; A-95; A-115 and A-406. 1 Publication
Mutagenesisi115 – 1151T → A: Abolishes phosphorylation; when associated with A-44; A-59; A-95; A-103 and A-406. 1 Publication
Mutagenesisi406 – 4061T → A: Abolishes phosphorylation; when associated with A-44; A-59; A-95; A-103 and A-115. 1 Publication
Mutagenesisi482 – 4821C → Y in CDC16-264; G2/M cell cycle arrest at 36 degrees Celsius. 1 Publication
Mutagenesisi530 – 5301S → P in CDC16-183; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication
Mutagenesisi557 – 5571S → F in CDC16-1; G2/M cell cycle arrest at 36 degrees Celsius. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 840840Anaphase-promoting complex subunit CDC16PRO_0000106269Add
BLAST

Post-translational modificationi

Phosphorylated by CDC28, which is required for the early mitotic activity of the APC/C in its CDC20-bound form.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP09798.
TopDownProteomicsiP09798.

PTM databases

iPTMnetiP09798.

Interactioni

Subunit structurei

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. Interacts with AMA1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DOC1P530687EBI-4208,EBI-2603

Protein-protein interaction databases

BioGridi34109. 46 interactions.
DIPiDIP-25N.
IntActiP09798. 27 interactions.
MINTiMINT-655181.

Structurei

3D structure databases

ProteinModelPortaliP09798.
SMRiP09798. Positions 205-753.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati229 – 26032TPR 1Add
BLAST
Repeati263 – 28826TPR 2Add
BLAST
Repeati296 – 31924TPR 3Add
BLAST
Repeati357 – 38832TPR 4Add
BLAST
Repeati393 – 41624TPR 5Add
BLAST
Repeati426 – 45429TPR 6Add
BLAST
Repeati464 – 49229TPR 7Add
BLAST
Repeati499 – 52628TPR 8Add
BLAST
Repeati531 – 56030TPR 9Add
BLAST
Repeati565 – 59329TPR 10Add
BLAST
Repeati600 – 62829TPR 11Add
BLAST
Repeati633 – 66533TPR 12Add
BLAST
Repeati671 – 70333TPR 13Add
BLAST
Repeati708 – 73730TPR 14Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi209 – 22012Poly-ThrAdd
BLAST

Sequence similaritiesi

Belongs to the APC6/CDC16 family.Curated
Contains 14 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

GeneTreeiENSGT00510000047327.
HOGENOMiHOG000160791.
InParanoidiP09798.
KOiK03353.
OMAiAHEICES.
OrthoDBiEOG7ZKSKQ.

Family and domain databases

Gene3Di1.25.40.10. 5 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF07719. TPR_2. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 8 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 4 hits.
PROSITEiPS50005. TPR. 7 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09798-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFCLYCCHC YIVICGKATH YYKSSKATSN LKSSNRVLMR NPMSPSEQHS
60 70 80 90 100
QHNSTLAASP FVSNVSAART QQSLPTDAQN DRLQQPWNRT NTATSPYQSL
110 120 130 140 150
ANSPLIQKLQ ANIMTPHQPS ANSNSNSNSI TGNVVNDNNL LASMSKNSMF
160 170 180 190 200
GSTIPSTLRK VSLQREYKDS VDGVVRDEDN DEDVHNNGDA AANANNDRES
210 220 230 240 250
KLGHNGPLTT TTLTTTTTAT QLDVSELSAI ERLRLWRFDA LMQHMYRTAE
260 270 280 290 300
YIADKVYNIS NDPDDAFWLG QVYYNNNQYV RAVELITRNN LDGVNILCRY
310 320 330 340 350
LLGLSFVKLQ RFDDALDVIG EYNPFSEDPS TTAANTMSNN GNNSNTSQPV
360 370 380 390 400
TDGGIKMESS LCFLRGKIYF AQNNFNKARD AFREAILVDI KNFEAFEMLL
410 420 430 440 450
SKNLLTPQEE WDLFDSLDFK EFGEDKEIMK NLYKINLSKY INTEDITKSN
460 470 480 490 500
EILAKDYKLA DNVDVVRSKV DICYTQCKFN ECLELCETVL ENDEFNTNIL
510 520 530 540 550
PAYIGCLYEL SNKNKLFLLS HRLAETFPKS AITWFSVATY YMSLDRISEA
560 570 580 590 600
QKYYSKSSIL DPSFAAAWLG FAHTYALEGE QDQALTAYST ASRFFPGMHL
610 620 630 640 650
PKLFLGMQFM AMNSLNLAES YFVLAYDICP NDPLVLNEMG VMYFKKNEFV
660 670 680 690 700
KAKKYLKKAL EVVKDLDPSS RTTISIQLNL GHTYRKLNEN EIAIKCFRCV
710 720 730 740 750
LEKNDKNSEI HCSLGYLYLK TKKLQKAIDH LHKSLYLKPN NSSATALLKN
760 770 780 790 800
ALELNVTLSL DASHPLIDKS NLMSQASKDK ASLNKKRSSL TYDPVNMAKR
810 820 830 840
LRTQKEIFDQ NNKALRKGGH DSKTGSNNAD DDFDADMELE
Length:840
Mass (Da):94,992
Last modified:July 1, 1989 - v1
Checksum:iA096B34441083488
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06165 Genomic DNA. Translation: CAA29521.1.
Z28022 Genomic DNA. Translation: CAA81857.1.
BK006944 Genomic DNA. Translation: DAA09133.1.
PIRiA27832.
RefSeqiNP_012903.1. NM_001179588.1.

Genome annotation databases

EnsemblFungiiYKL022C; YKL022C; YKL022C.
GeneIDi853846.
KEGGisce:YKL022C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06165 Genomic DNA. Translation: CAA29521.1.
Z28022 Genomic DNA. Translation: CAA81857.1.
BK006944 Genomic DNA. Translation: DAA09133.1.
PIRiA27832.
RefSeqiNP_012903.1. NM_001179588.1.

3D structure databases

ProteinModelPortaliP09798.
SMRiP09798. Positions 205-753.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34109. 46 interactions.
DIPiDIP-25N.
IntActiP09798. 27 interactions.
MINTiMINT-655181.

PTM databases

iPTMnetiP09798.

Proteomic databases

MaxQBiP09798.
TopDownProteomicsiP09798.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL022C; YKL022C; YKL022C.
GeneIDi853846.
KEGGisce:YKL022C.

Organism-specific databases

EuPathDBiFungiDB:YKL022C.
SGDiS000001505. CDC16.

Phylogenomic databases

GeneTreeiENSGT00510000047327.
HOGENOMiHOG000160791.
InParanoidiP09798.
KOiK03353.
OMAiAHEICES.
OrthoDBiEOG7ZKSKQ.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciYEAST:G3O-31830-MONOMER.

Miscellaneous databases

PROiP09798.

Family and domain databases

Gene3Di1.25.40.10. 5 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF07719. TPR_2. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 8 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 4 hits.
PROSITEiPS50005. TPR. 7 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Metal-binding, nucleic acid-binding finger sequences in the CDC16 gene of Saccharomyces cerevisiae."
    Icho T., Wickner R.B.
    Nucleic Acids Res. 15:8439-8450(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: R.B.Wickner 1385.
  2. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  5. "CDC16 controls initiation at chromosome replication origins."
    Heichman K.A., Roberts J.M.
    Mol. Cell 1:457-463(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-482 AND SER-557.
  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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION BY CDC28, MUTAGENESIS OF SER-44; SER-59; SER-95; SER-103; THR-115 AND THR-406.
  7. "Ama1p is a meiosis-specific regulator of the anaphase promoting complex/cyclosome in yeast."
    Cooper K.F., Mallory M.J., Egeland D.B., Jarnik M., Strich R.
    Proc. Natl. Acad. Sci. U.S.A. 97:14548-14553(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AMA1.
  8. "A novel yeast mutant that is defective in regulation of the Anaphase-Promoting Complex by the spindle damage checkpoint."
    Lai L.A., Morabito L., Holloway S.L.
    Mol. Genet. Genomics 270:156-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF SER-530.
  9. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  10. "A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis."
    Sikorski R.S., Boguski M.S., Goebl M., Hieter P.A.
    Cell 60:307-317(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS TPR REPEATS.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "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].
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCDC16_YEAST
AccessioniPrimary (citable) accession number: P09798
Secondary accession number(s): D6VXR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 8, 2016
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2753 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: 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.