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Protein

Cell division cycle protein 16 homolog

Gene

Cdc16

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).By similarity

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

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-MMU-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-MMU-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-MMU-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-MMU-176412. Phosphorylation of the APC/C.
R-MMU-179409. APC-Cdc20 mediated degradation of Nek2A.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2559582. Senescence-Associated Secretory Phenotype (SASP).
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division cycle protein 16 homolog
Alternative name(s):
Anaphase-promoting complex subunit 6
Short name:
APC6
Cyclosome subunit 6
Gene namesi
Name:Cdc16
Synonyms:Anapc6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1917207. Cdc16.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: UniProtKB
  • centrosome Source: MGI
  • cytoplasm Source: MGI
  • nucleus Source: MGI
  • spindle microtubule Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 620620Cell division cycle protein 16 homologPRO_0000106268Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei490 – 4901PhosphoserineBy similarity
Modified residuei560 – 5601PhosphoserineCombined sources
Modified residuei599 – 5991PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylated. Phosphorylation on Ser-560 occurs specifically during mitosis (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8R349.
MaxQBiQ8R349.
PaxDbiQ8R349.
PRIDEiQ8R349.

PTM databases

iPTMnetiQ8R349.
PhosphoSiteiQ8R349.

Expressioni

Gene expression databases

BgeeiQ8R349.
ExpressionAtlasiQ8R349. baseline and differential.
GenevisibleiQ8R349. MM.

Interactioni

Subunit structurei

V-shaped homodimer. Interacts with CDC26. The mammalian APC/C is composed of 14 distinct subunits that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa. Interacts with PPP5C and CDC20 (By similarity).By similarity

Protein-protein interaction databases

BioGridi213776. 47 interactions.
IntActiQ8R349. 50 interactions.
MINTiMINT-4090351.
STRINGi10090.ENSMUSP00000047950.

Structurei

3D structure databases

ProteinModelPortaliQ8R349.
SMRiQ8R349. Positions 2-533.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati4 – 3330TPR 1Add
BLAST
Repeati37 – 6226TPR 2Add
BLAST
Repeati70 – 9324TPR 3Add
BLAST
Repeati128 – 15932TPR 4Add
BLAST
Repeati164 – 18724TPR 5Add
BLAST
Repeati198 – 22225TPR 6Add
BLAST
Repeati232 – 26029TPR 7Add
BLAST
Repeati267 – 29428TPR 8Add
BLAST
Repeati299 – 32931TPR 9Add
BLAST
Repeati334 – 36229TPR 10Add
BLAST
Repeati369 – 39729TPR 11Add
BLAST
Repeati402 – 43433TPR 12Add
BLAST
Repeati442 – 47433TPR 13Add
BLAST
Repeati479 – 50830TPR 14Add
BLAST

Domaini

TPR repeats 1-7 mediate homodimerization, while the C-terminal TPR repeats bind to CDC26, burying its hydrophobic N-terminus.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1173. Eukaryota.
ENOG410XNY1. LUCA.
GeneTreeiENSGT00510000047327.
HOGENOMiHOG000230908.
HOVERGENiHBG050857.
InParanoidiQ8R349.
KOiK03353.
OMAiFIDMRRY.
OrthoDBiEOG72VH5N.
PhylomeDBiQ8R349.
TreeFamiTF101054.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
SMARTiSM00028. TPR. 6 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 4 hits.
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R349-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLEPLRKRV RQYLDQQQYQ SALFWADKVA SLSHEEPQDV YWLAQCLYLT
60 70 80 90 100
AQYHRAAHAL RSRKLDKLYE ACRYLAARCH YAAKEHQQAL DILDMEEPIN
110 120 130 140 150
RRLFEKYLKD DNGSRDPSSD WEMSQSSIKS SICLLRGKIY DALDNRTLAT
160 170 180 190 200
YSYKEALKLD VYCFEAFDLL TSHHMLTAQE EKELLDSLPL NKLCAEEQEL
210 220 230 240 250
LRFVFENKLK KYNKPSETVI PESVDGLQEN LDVVVSLAER HYYNCDFKMC
260 270 280 290 300
YKLTSTVMEK DPFHANCLPV HIGTLVELNK ANELFYLSHK LVDLYPSNPV
310 320 330 340 350
SWFAVGCYYL MVGHKNEHAR RYLSKATTLE KTYGPAWIAY GHSFAVESEH
360 370 380 390 400
DQAMAAYFTA AQLMKGCHLP MLYIGLEYGL TNNSKLAERF FGQALSIAPE
410 420 430 440 450
DPFVIHEVGV VAFQNGEWKT AEKWFLDALE KIKAIGNEVT VDKWEPLLNN
460 470 480 490 500
LGHVCRKLKK YAEALDYHRQ ALVLIPQNAS TYSAIGYIHS LMGNFENAVD
510 520 530 540 550
YFHTALGLRR DDTFSVTMLG HCIEMYIGDS EAYIGADIKD KLKCYDFDVH
560 570 580 590 600
TMKTLKNIIS PPWDFRDFEV EKQNTEEAGL APLQNSTKAP ESRPNLEETF
610 620
EIEMNESDMM LETSMSDHST
Length:620
Mass (Da):71,460
Last modified:June 1, 2002 - v1
Checksum:iA0E47748506CC14E
GO

Sequence cautioni

The sequence BAB28717.1 differs from that shown.Intron retention.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC026606 mRNA. Translation: AAH26606.1.
AK013213 mRNA. Translation: BAB28717.1. Sequence problems.
CCDSiCCDS22114.1.
RefSeqiNP_081552.2. NM_027276.2.
UniGeneiMm.182412.

Genome annotation databases

EnsembliENSMUST00000043962; ENSMUSP00000047950; ENSMUSG00000038416.
GeneIDi69957.
KEGGimmu:69957.
UCSCiuc009kyi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC026606 mRNA. Translation: AAH26606.1.
AK013213 mRNA. Translation: BAB28717.1. Sequence problems.
CCDSiCCDS22114.1.
RefSeqiNP_081552.2. NM_027276.2.
UniGeneiMm.182412.

3D structure databases

ProteinModelPortaliQ8R349.
SMRiQ8R349. Positions 2-533.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213776. 47 interactions.
IntActiQ8R349. 50 interactions.
MINTiMINT-4090351.
STRINGi10090.ENSMUSP00000047950.

PTM databases

iPTMnetiQ8R349.
PhosphoSiteiQ8R349.

Proteomic databases

EPDiQ8R349.
MaxQBiQ8R349.
PaxDbiQ8R349.
PRIDEiQ8R349.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043962; ENSMUSP00000047950; ENSMUSG00000038416.
GeneIDi69957.
KEGGimmu:69957.
UCSCiuc009kyi.1. mouse.

Organism-specific databases

CTDi8881.
MGIiMGI:1917207. Cdc16.

Phylogenomic databases

eggNOGiKOG1173. Eukaryota.
ENOG410XNY1. LUCA.
GeneTreeiENSGT00510000047327.
HOGENOMiHOG000230908.
HOVERGENiHBG050857.
InParanoidiQ8R349.
KOiK03353.
OMAiFIDMRRY.
OrthoDBiEOG72VH5N.
PhylomeDBiQ8R349.
TreeFamiTF101054.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-MMU-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-MMU-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-MMU-176412. Phosphorylation of the APC/C.
R-MMU-179409. APC-Cdc20 mediated degradation of Nek2A.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2559582. Senescence-Associated Secretory Phenotype (SASP).

Miscellaneous databases

ChiTaRSiCdc16. mouse.
PROiQ8R349.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R349.
ExpressionAtlasiQ8R349. baseline and differential.
GenevisibleiQ8R349. MM.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
SMARTiSM00028. TPR. 6 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 4 hits.
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 325-620.
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCDC16_MOUSE
AccessioniPrimary (citable) accession number: Q8R349
Secondary accession number(s): Q9CYX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: June 1, 2002
Last modified: July 6, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.