Q12834 · CDC20_HUMAN
- ProteinCell division cycle protein 20 homolog
- GeneCDC20
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids499 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the metaphase/anaphase transition of cell cycle (PubMed:32666501).
Required for full ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) and confers substrate specificity upon the complex (PubMed:27030811).
Is regulated by MAD2L1: in metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic differentiation. The CDC20-APC/C complex promotes proper dilation formation and radial migration by degrading CCDC41 (By similarity).
Required for full ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) and confers substrate specificity upon the complex (PubMed:27030811).
Is regulated by MAD2L1: in metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic differentiation. The CDC20-APC/C complex promotes proper dilation formation and radial migration by degrading CCDC41 (By similarity).
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 | |||
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Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCell division cycle protein 20 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 accessionQ12834
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Oocyte/zygote/embryo maturation arrest 14 (OZEMA14)
- Note
- DescriptionAn autosomal recessive female infertility disorder characterized by oocyte maturation arrest, fertilization failure, and/or early embryonic arrest.
- See alsoMIM:620276
Natural variants in OZEMA14
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_088388 | 182-499 | missing | in OZEMA14; severely decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; fails to localize to the kinetochore | |
VAR_088389 | 211 | A>T | in OZEMA14; uncertain significance | |
VAR_088390 | 228 | Y>C | in OZEMA14; decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; shows normal kinetochore localization | |
VAR_088391 | 262-499 | missing | in OZEMA14; dbSNP:rs754957702 | |
VAR_088393 | 296 | R>Q | in OZEMA14; uncertain significance; decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; shows normal kinetochore localization | |
VAR_088395 | 322 | R>Q | in OZEMA14; severely decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; shows normal kinetochore localization | |
VAR_088394 | 322-499 | missing | in OZEMA14; severely decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; fails to localize to the kinetochore | |
VAR_088396 | 385 | W>C | in OZEMA14; decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; slightly decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; shows normal kinetochore localization | |
VAR_088397 | 439 | L>R | in OZEMA14; uncertain significance; decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; shows normal kinetochore localization |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 41 | Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-72; A-92; A-153; A-157 and A-161. | ||||
Sequence: S → A | ||||||
Mutagenesis | 72 | Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-41; A-92; A-153; A-157 and A-161. | ||||
Sequence: S → A | ||||||
Mutagenesis | 92 | Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-41; A-72; A-153; A-157 and A-161. | ||||
Sequence: S → A | ||||||
Mutagenesis | 132 | Loss of interaction with MAD2L1. | ||||
Sequence: R → A | ||||||
Mutagenesis | 153 | Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-42; A-72; A-92; A-157 and A-161. | ||||
Sequence: S → A | ||||||
Mutagenesis | 157 | Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-42; A-72; A-92; A-153 and A-161. | ||||
Sequence: T → A | ||||||
Mutagenesis | 161 | Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-72; A-92; A-153; A-157 and A-161. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_088388 | 182-499 | in OZEMA14; severely decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; fails to localize to the kinetochore | |||
Sequence: Missing | ||||||
Natural variant | VAR_088389 | 211 | in OZEMA14; uncertain significance | |||
Sequence: A → T | ||||||
Natural variant | VAR_088390 | 228 | in OZEMA14; decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; shows normal kinetochore localization | |||
Sequence: Y → C | ||||||
Natural variant | VAR_088391 | 262-499 | in OZEMA14; dbSNP:rs754957702 | |||
Sequence: Missing | ||||||
Natural variant | VAR_088392 | 286 | found in a patient with mosaic variagated aneuploidy syndrome 1; uncertain significance; decreased interaction with BUB1B during the formation of the mitotic checkpoint complex; shows normal kinetochore localization | |||
Sequence: R → S | ||||||
Natural variant | VAR_088393 | 296 | in OZEMA14; uncertain significance; decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; shows normal kinetochore localization | |||
Sequence: R → Q | ||||||
Natural variant | VAR_088395 | 322 | in OZEMA14; severely decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; shows normal kinetochore localization | |||
Sequence: R → Q | ||||||
Natural variant | VAR_088394 | 322-499 | in OZEMA14; severely decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; fails to localize to the kinetochore | |||
Sequence: Missing | ||||||
Natural variant | VAR_088396 | 385 | in OZEMA14; decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; slightly decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; shows normal kinetochore localization | |||
Sequence: W → C | ||||||
Natural variant | VAR_030368 | 402 | in dbSNP:rs45443196 | |||
Sequence: V → M | ||||||
Natural variant | VAR_088397 | 439 | in OZEMA14; uncertain significance; decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; shows normal kinetochore localization | |||
Sequence: L → R | ||||||
Natural variant | VAR_030369 | 479 | in dbSNP:rs45461499 | |||
Sequence: R → Q | ||||||
Mutagenesis | 485 | Does not affect its ability to bind the APC/C complex; when associated with R-490. | ||||
Sequence: K → R | ||||||
Mutagenesis | 490 | Does not affect its ability to bind the APC/C complex; when associated with R-485. | ||||
Sequence: K → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 541 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000050900 | 1-499 | UniProt | Cell division cycle protein 20 homolog | |||
Sequence: MAQFAFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYIPHRSAAQMEVASFLLSKENQPENSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGSSRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGEYISSVAWIKEGNYLAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPDGRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHSQVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARRREREKASAAKSSLIHQGIR | |||||||
Modified residue | 41 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 41 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 59 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 66 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 69 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 70 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 70 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 72 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 72 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 92 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 104 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 106 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 106 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 108 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 134 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 153 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 157 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 157 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 161 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 485 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 490 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Acetylated. Deacetylated at Lys-66 by SIRT2; deacetylation enhances the interaction of CDC20 with CDC27, leading to activation of anaphase promoting complex/cyclosome (APC/C).
Phosphorylated during mitosis (PubMed:14657031).
Phosphorylated by BUB1 at Ser-41; Ser-72; Ser-92; Ser-153; Thr-157 and Ser-161 (PubMed:15525512).
Phosphorylated by NEK2 (PubMed:20034488).
Phosphorylated by BUB1 at Ser-41; Ser-72; Ser-92; Ser-153; Thr-157 and Ser-161 (PubMed:15525512).
Phosphorylated by NEK2 (PubMed:20034488).
Dephosphorylated by CTDP1.
Ubiquitinated and degraded by the proteasome during spindle assembly checkpoint (PubMed:18997788, PubMed:19098431).
Deubiquitinated by USP44, leading to stabilize the MAD2L1-CDC20-APC/C ternary complex, thereby preventing premature activation of the APC/C (PubMed:17443180).
Ubiquitinated at Lys-490 during prometaphase (PubMed:21926987).
Ubiquitination at Lys-485 and Lys-490 has no effect on its ability to bind the APC/C complex (PubMed:21926987).
Ubiquitinated by UBR5 when not assembled in a multiprotein complex, leading to its degradation: UBR5 recognizes and binds a degron that is not accessible when CDC20 is part of a complex (PubMed:35217622, PubMed:37478862).
Deubiquitinated by USP44, leading to stabilize the MAD2L1-CDC20-APC/C ternary complex, thereby preventing premature activation of the APC/C (PubMed:17443180).
Ubiquitinated at Lys-490 during prometaphase (PubMed:21926987).
Ubiquitination at Lys-485 and Lys-490 has no effect on its ability to bind the APC/C complex (PubMed:21926987).
Ubiquitinated by UBR5 when not assembled in a multiprotein complex, leading to its degradation: UBR5 recognizes and binds a degron that is not accessible when CDC20 is part of a complex (PubMed:35217622, PubMed:37478862).
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of a complex with CDC20, CDC27, SPATC1 and TUBG1 (By similarity).
Interacts with NEUROD2 (By similarity).
Interacts with dimeric MAD2L1 in its closed conformation form (PubMed:15525512, PubMed:19098431, PubMed:29162720, PubMed:9637688, PubMed:9811605).
Interacts with BUB1B (PubMed:15525512, PubMed:18997788, PubMed:19098431, PubMed:33094908).
The phosphorylated form interacts with APC/C (PubMed:9637688, PubMed:9734353, PubMed:9811605).
Interacts with NINL (PubMed:17403670).
May interact with MAD2L2 (PubMed:11459826).
Interacts with CDK5RAP2 (PubMed:19282672).
Interacts with SIRT2 (PubMed:22014574).
Interacts with isoform 1 of NEK2 (PubMed:20034488).
Interacts with HSF1 (via phosphorylated form); this interaction occurs in mitosis in a MAD2L1-dependent manner and prevents PLK1-stimulated degradation of HSF1 by blocking the recruitment of the SCF(BTRC) ubiquitin ligase complex (PubMed:18794143).
Interacts (via the N-terminal substrate-binding domain) with FBXO5 (By similarity).
Interacts with CCNF (PubMed:27653696).
Interacts with USP22 (PubMed:27030811).
Interacts with NEUROD2 (By similarity).
Interacts with dimeric MAD2L1 in its closed conformation form (PubMed:15525512, PubMed:19098431, PubMed:29162720, PubMed:9637688, PubMed:9811605).
Interacts with BUB1B (PubMed:15525512, PubMed:18997788, PubMed:19098431, PubMed:33094908).
The phosphorylated form interacts with APC/C (PubMed:9637688, PubMed:9734353, PubMed:9811605).
Interacts with NINL (PubMed:17403670).
May interact with MAD2L2 (PubMed:11459826).
Interacts with CDK5RAP2 (PubMed:19282672).
Interacts with SIRT2 (PubMed:22014574).
Interacts with isoform 1 of NEK2 (PubMed:20034488).
Interacts with HSF1 (via phosphorylated form); this interaction occurs in mitosis in a MAD2L1-dependent manner and prevents PLK1-stimulated degradation of HSF1 by blocking the recruitment of the SCF(BTRC) ubiquitin ligase complex (PubMed:18794143).
Interacts (via the N-terminal substrate-binding domain) with FBXO5 (By similarity).
Interacts with CCNF (PubMed:27653696).
Interacts with USP22 (PubMed:27030811).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q12834 | ANAPC4 Q9UJX5 | 10 | EBI-367462, EBI-2554854 | |
XENO | Q12834 | Axin2 O88566 | 2 | EBI-367462, EBI-7690990 | |
BINARY | Q12834 | BUB1B O60566 | 38 | EBI-367462, EBI-1001438 | |
BINARY | Q12834 | CDC27 P30260 | 14 | EBI-367462, EBI-994813 | |
BINARY | Q12834 | MAD2L1 Q13257 | 38 | EBI-367462, EBI-78203 | |
BINARY | Q12834 | MAD2L2 Q9UI95 | 2 | EBI-367462, EBI-77889 | |
BINARY | Q12834 | RASSF1 Q9NS23-2 | 2 | EBI-367462, EBI-438698 | |
BINARY | Q12834 | SIRT2 Q8IXJ6-2 | 2 | EBI-367462, EBI-5240785 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 17-80 | Disordered | ||||
Sequence: DAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYI | ||||||
Compositional bias | 52-72 | Polar residues | ||||
Sequence: AGRTPGRTPGKSSSKVQTTPS | ||||||
Repeat | 182-221 | WD 1 | ||||
Sequence: RNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQ | ||||||
Repeat | 224-263 | WD 2 | ||||
Sequence: QPGEYISSVAWIKEGNYLAVGTSSAEVQLWDVQQQKRLRN | ||||||
Repeat | 266-303 | WD 3 | ||||
Sequence: SHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVA | ||||||
Repeat | 307-346 | WD 4 | ||||
Sequence: GHSQEVCGLRWAPDGRHLASGGNDNLVNVWPSAPGEGGWV | ||||||
Repeat | 353-395 | WD 5 | ||||
Sequence: QHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSA | ||||||
Repeat | 397-438 | WD 6 | ||||
Sequence: DAHSQVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAE | ||||||
Repeat | 441-480 | WD 7 | ||||
Sequence: GHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARR |
Sequence similarities
Belongs to the WD repeat CDC20/Fizzy family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length499
- Mass (Da)54,723
- Last updated2003-10-03 v2
- ChecksumFD5C967AF84089E8
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 52-72 | Polar residues | ||||
Sequence: AGRTPGRTPGKSSSKVQTTPS | ||||||
Sequence conflict | 101 | in Ref. 1; AAA19017 | ||||
Sequence: P → S | ||||||
Sequence conflict | 117 | in Ref. 8; AAH00624 | ||||
Sequence: A → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U05340 EMBL· GenBank· DDBJ | AAA19017.1 EMBL· GenBank· DDBJ | mRNA | ||
AF099644 EMBL· GenBank· DDBJ | AAD16405.1 EMBL· GenBank· DDBJ | mRNA | ||
AK312780 EMBL· GenBank· DDBJ | BAG35643.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007388 EMBL· GenBank· DDBJ | AAP36052.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ473545 EMBL· GenBank· DDBJ | ABE96834.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL139289 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471059 EMBL· GenBank· DDBJ | EAX07101.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471059 EMBL· GenBank· DDBJ | EAX07102.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000624 EMBL· GenBank· DDBJ | AAH00624.1 EMBL· GenBank· DDBJ | mRNA | ||
BC001088 EMBL· GenBank· DDBJ | AAH01088.1 EMBL· GenBank· DDBJ | mRNA | ||
BC006272 EMBL· GenBank· DDBJ | AAH06272.1 EMBL· GenBank· DDBJ | mRNA | ||
BC009425 EMBL· GenBank· DDBJ | AAH09425.1 EMBL· GenBank· DDBJ | mRNA | ||
BC009426 EMBL· GenBank· DDBJ | AAH09426.1 EMBL· GenBank· DDBJ | mRNA | ||
BC010044 EMBL· GenBank· DDBJ | AAH10044.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012803 EMBL· GenBank· DDBJ | AAH12803.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012827 EMBL· GenBank· DDBJ | AAH12827.1 EMBL· GenBank· DDBJ | mRNA | ||
BC013303 EMBL· GenBank· DDBJ | AAH13303.1 EMBL· GenBank· DDBJ | mRNA | ||
BC015998 EMBL· GenBank· DDBJ | AAH15998.1 EMBL· GenBank· DDBJ | mRNA | ||
BC024257 EMBL· GenBank· DDBJ | AAH24257.1 EMBL· GenBank· DDBJ | mRNA | ||
BC031294 EMBL· GenBank· DDBJ | AAH31294.1 EMBL· GenBank· DDBJ | mRNA | ||
BC110321 EMBL· GenBank· DDBJ | AAI10322.1 EMBL· GenBank· DDBJ | mRNA |