Q9UJX2 · CDC23_HUMAN
- ProteinCell division cycle protein 23 homolog
- GeneCDC23
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids597 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 (PubMed:18485873).
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 (PubMed:18485873).
The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132).
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 (PubMed:18485873).
The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132).
Pathway
Protein modification; protein ubiquitination.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | anaphase-promoting complex | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | anaphase-promoting complex-dependent catabolic process | |
Biological Process | cell division | |
Biological Process | metaphase/anaphase transition of mitotic cell cycle | |
Biological Process | mitotic cell cycle | |
Biological Process | mitotic metaphase chromosome alignment | |
Biological Process | positive regulation of mitotic metaphase/anaphase transition | |
Biological Process | protein branched polyubiquitination | |
Biological Process | protein K11-linked ubiquitination | |
Biological Process | protein K48-linked ubiquitination | |
Biological Process | protein ubiquitination | |
Biological Process | regulation of exit from mitosis | |
Biological Process | regulation of meiotic cell cycle | |
Biological Process | regulation of mitotic cell cycle | |
Biological Process | regulation of mitotic metaphase/anaphase transition | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCell division cycle protein 23 homolog
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UJX2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_024675 | 9 | in dbSNP:rs2231471 | |||
Sequence: P → L | ||||||
Natural variant | VAR_019232 | 78 | in dbSNP:rs17228304 | |||
Sequence: E → Q | ||||||
Mutagenesis | 339 | Inhibits APC/FZR1 E3 ubiquitin-protein ligase complex activity; when associated with A-374. | ||||
Sequence: N → A | ||||||
Mutagenesis | 374 | Inhibits APC/FZR1 E3 ubiquitin-protein ligase complex activity; when associated with A-339. | ||||
Sequence: E → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 445 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000106270 | 2-597 | UniProt | Cell division cycle protein 23 homolog | |||
Sequence: AASTSMVPVAVTAAVAPVLSINSDFSDLREIKKQLLLIAGLTRERGLLHSSKWSAELAFSLPALPLAELQPPPPITEEDAQDMDAYTLAKAYFDVKEYDRAAHFLHGCNSKKAYFLYMYSRYLSGEKKKDDETVDSLGPLEKGQVKNEALRELRVELSKKHQARELDGFGLYLYGVVLRKLDLVKEAIDVFVEATHVLPLHWGAWLELCNLITDKEMLKFLSLPDTWMKEFFLAHIYTELQLIEEALQKYQNLIDVGFSKSSYIVSQIAVAYHNIRDIDKALSIFNELRKQDPYRIENMDTFSNLLYVRSMKSELSYLAHNLCEIDKYRVETCCVIGNYYSLRSQHEKAALYFQRALKLNPRYLGAWTLMGHEYMEMKNTSAAIQAYRHAIEVNKRDYRAWYGLGQTYEILKMPFYCLYYYRRAHQLRPNDSRMLVALGECYEKLNQLVEAKKCYWRAYAVGDVEKMALVKLAKLHEQLTESEQAAQCYIKYIQDIYSCGEIVEHLEESTAFRYLAQYYFKCKLWDEASTCAQKCCAFNDTREEGKALLRQILQLRNQGETPTTEVPAPFFLPASLSANNTPTRRVSPLNLSSVTP | |||||||
Cross-link | 147 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 273 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 467 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 530 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 542 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 562 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 562 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 565 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 565 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 576 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 578 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 578 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 582 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 582 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 584 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 588 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 588 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 593 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 593 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 594 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 596 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 596 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated. Phosphorylation on Thr-562 occurs specifically during mitosis.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. Interacts with FBXO43; the interaction is direct.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 27-63 | TPR 1 | ||||
Sequence: SDLREIKKQLLLIAGLTRERGLLHSSKWSAELAFSLP | ||||||
Repeat | 73-112 | TPR 2 | ||||
Sequence: PPPITEEDAQDMDAYTLAKAYFDVKEYDRAAHFLHGCNSK | ||||||
Repeat | 114-144 | TPR 3 | ||||
Sequence: AYFLYMYSRYLSGEKKKDDETVDSLGPLEKG | ||||||
Repeat | 169-200 | TPR 4 | ||||
Sequence: GFGLYLYGVVLRKLDLVKEAIDVFVEATHVLP | ||||||
Repeat | 229-259 | TPR 5 | ||||
Sequence: MKEFFLAHIYTELQLIEEALQKYQNLIDVGF | ||||||
Repeat | 263-293 | TPR 6 | ||||
Sequence: SYIVSQIAVAYHNIRDIDKALSIFNELRKQD | ||||||
Repeat | 297-327 | TPR 7 | ||||
Sequence: IENMDTFSNLLYVRSMKSELSYLAHNLCEID | ||||||
Repeat | 331-361 | TPR 8 | ||||
Sequence: VETCCVIGNYYSLRSQHEKAALYFQRALKLN | ||||||
Repeat | 366-395 | TPR 9 | ||||
Sequence: GAWTLMGHEYMEMKNTSAAIQAYRHAIEVN | ||||||
Repeat | 400-432 | TPR 10 | ||||
Sequence: RAWYGLGQTYEILKMPFYCLYYYRRAHQLRPND | ||||||
Repeat | 433-466 | TPR 11 | ||||
Sequence: SRMLVALGECYEKLNQLVEAKKCYWRAYAVGDVE | ||||||
Repeat | 468-500 | TPR 12 | ||||
Sequence: MALVKLAKLHEQLTESEQAAQCYIKYIQDIYSC | ||||||
Repeat | 504-540 | TPR 13 | ||||
Sequence: VEHLEESTAFRYLAQYYFKCKLWDEASTCAQKCCAFN |
Sequence similarities
Belongs to the APC8/CDC23 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9UJX2-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length597
- Mass (Da)68,834
- Last updated2009-07-28 v3
- Checksum358F2B8745DB9D32
Q9UJX2-2
- Name2
Q9UJX2-3
- Name3
- Differences from canonical
- 1-118: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_037678 | 1-118 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 83 | in Ref. 4; BAD96970 | ||||
Sequence: D → E | ||||||
Sequence conflict | 105 | in Ref. 4; BAD96970 | ||||
Sequence: F → S | ||||||
Alternative sequence | VSP_008429 | 125-151 | in isoform 2 | |||
Sequence: SGEKKKDDETVDSLGPLEKGQVKNEAL → VRAILKCHSAFSETSIFRTNGKVKSFK | ||||||
Alternative sequence | VSP_008430 | 152-597 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 527 | in Ref. 2; BAG65414 | ||||
Sequence: D → G | ||||||
Sequence conflict | 588 | in Ref. 9; AAF05755 | ||||
Sequence: S → F |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB011472 EMBL· GenBank· DDBJ | BAA75628.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK291610 EMBL· GenBank· DDBJ | BAF84299.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK304635 EMBL· GenBank· DDBJ | BAG65414.1 EMBL· GenBank· DDBJ | mRNA | ||
AY603103 EMBL· GenBank· DDBJ | AAS99353.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
AK223250 EMBL· GenBank· DDBJ | BAD96970.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC106752 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471062 EMBL· GenBank· DDBJ | EAW62155.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471062 EMBL· GenBank· DDBJ | EAW62154.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471062 EMBL· GenBank· DDBJ | EAW62156.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC005258 EMBL· GenBank· DDBJ | AAH05258.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC010944 EMBL· GenBank· DDBJ | AAH10944.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC017713 EMBL· GenBank· DDBJ | AAH17713.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF053977 EMBL· GenBank· DDBJ | AAC70920.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF191341 EMBL· GenBank· DDBJ | AAF05755.1 EMBL· GenBank· DDBJ | mRNA | ||
BT009810 EMBL· GenBank· DDBJ | AAP88812.1 EMBL· GenBank· DDBJ | mRNA |