Q2KHM9 · MOONR_HUMAN
- ProteinProtein moonraker
- GeneKIAA0753
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids967 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in centriole duplication (PubMed:24613305, PubMed:26297806).
Positively regulates CEP63 centrosomal localization (PubMed:24613305, PubMed:26297806).
Required for WDR62 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:24613305, PubMed:26297806).
May play a role in cilium assembly
Positively regulates CEP63 centrosomal localization (PubMed:24613305, PubMed:26297806).
Required for WDR62 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:24613305, PubMed:26297806).
May play a role in cilium assembly
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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Aspect | Term | |
---|---|---|
Cellular Component | centriolar satellite | |
Cellular Component | centriole | |
Cellular Component | centrosome | |
Cellular Component | cytosol | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Biological Process | centriole replication | |
Biological Process | cilium assembly | |
Biological Process | cytosolic ciliogenesis | |
Biological Process | protein localization to centrosome |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein moonraker
- Short namesMNR
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ2KHM9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localization to centrioles and pericentriolar satellites may be mediated by interaction with PCM1.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Orofaciodigital syndrome 15 (OFD15)
- Note
- DescriptionA form of orofaciodigital syndrome, a group of heterogeneous disorders characterized by malformations of the oral cavity, face and digits, and associated phenotypic abnormalities that lead to the delineation of various subtypes. OFD15 features include facial dysmorphism, lobulated tongue, clefting of the alveolar ridges, left hand postaxial polydactyly, broad right hallux and left hallux duplication, and intermittent respiratory difficulty. Brain anomalies include vermis hypoplasia with molar tooth sign, agenesis of corpus callosum, and ventricular dilation. OFD15 inheritance is autosomal recessive.
- See alsoMIM:617127
Natural variants in OFD15
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086268 | 631-967 | missing | in OFD15 |
Joubert syndrome 38 (JBTS38)
- Note
- DescriptionA form of Joubert syndrome, a disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy, renal disease, liver fibrosis, and polydactyly. JBTS38 inheritance is autosomal recessive.
- See alsoMIM:619476
Natural variants in JBTS38
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_079381 | 257 | R>G | in JBTS38; uncertain significance; dbSNP:rs2150895254 |
Short-rib thoracic dysplasia 21 without polydactyly (SRTD21)
- Note
- DescriptionA form of short-rib thoracic dysplasia, a group of autosomal recessive ciliopathies that are characterized by a constricted thoracic cage, short ribs, shortened tubular bones, and a 'trident' appearance of the acetabular roof. Polydactyly is variably present. Non-skeletal involvement can include cleft lip/palate as well as anomalies of major organs such as the brain, eye, heart, kidneys, liver, pancreas, intestines, and genitalia. Some forms of the disease are lethal in the neonatal period due to respiratory insufficiency secondary to a severely restricted thoracic cage, whereas others are compatible with life. Disease spectrum encompasses Ellis-van Creveld syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-Saldino syndrome, and short rib-polydactyly syndrome.
- See alsoMIM:619479
Natural variants in SRTD21
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086266 | 315-967 | missing | in SRTD21 | |
VAR_086267 | 324-967 | missing | in SRTD21 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_031065 | 201 | in dbSNP:rs16955985 | |||
Sequence: H → Q | ||||||
Natural variant | VAR_079381 | 257 | in JBTS38; uncertain significance; dbSNP:rs2150895254 | |||
Sequence: R → G | ||||||
Natural variant | VAR_086266 | 315-967 | in SRTD21 | |||
Sequence: Missing | ||||||
Natural variant | VAR_086267 | 324-967 | in SRTD21 | |||
Sequence: Missing | ||||||
Natural variant | VAR_031066 | 375 | in dbSNP:rs9889363 | |||
Sequence: E → D | ||||||
Natural variant | VAR_031067 | 375 | in dbSNP:rs17794522 | |||
Sequence: E → G | ||||||
Natural variant | VAR_031068 | 444 | in dbSNP:rs2289643 | |||
Sequence: D → N | ||||||
Natural variant | VAR_031069 | 466 | in dbSNP:rs2289642 | |||
Sequence: L → P | ||||||
Natural variant | VAR_031070 | 501 | in dbSNP:rs11868877 | |||
Sequence: V → M | ||||||
Natural variant | VAR_031071 | 566 | in dbSNP:rs2304977 | |||
Sequence: P → L | ||||||
Natural variant | VAR_086268 | 631-967 | in OFD15 | |||
Sequence: Missing | ||||||
Natural variant | VAR_031072 | 896 | in dbSNP:rs1443417 | |||
Sequence: Q → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,145 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000280109 | 1-967 | UniProt | Protein moonraker | |||
Sequence: MGPGQPASTCVHLAPRTQLDGRSDPKVLQTQNQLQFNRNVPTHSSNLAIRYSCPHAIRIEKLKHSYNESYHCKDADCRVGPDLGSSVSFSVISQERLSYAVHLARRDVKRRQFEKHIKEHHLRSQPQSSQKCGHTKYKIPDHRVERKESKSQAACQCSHQPSKVEISSSGAKVYLYSSHPGQSDLTVPNSPPTHDPGLQPHPRIGDHKNISEQKSLLEVQRLQKELSSCIHKIEEVTKKDRLEEALDPDEERRIRIRRQEQAARSARMLYVLQQQVKEIQEELDKLSPHKIKHTKKSWAMSKLAAAHRGAIRALQMFVTQFTDRGEHPLPARCKELGSLIRQLSLCSVKLDADPSVPDVVIDILQQIEALESLLEKKLSPKKVKKCFSEIRSRFPIGSQKALERWPSTSPKGERRPLTAKDTFPQETSRPSVAKQLLADKYQPDTELPETQRLQSELDVLDADIVLEEGPFILDQSASFKDEVLAVAKTKAGKKKPVTENVPFRKKDTLAPARQQGLRKAERGRQSQPHSKSRVQQTTVSSRLKMNRQPVKDRKAPWIPPNPTSPPASPKCAAWLKVKTSPRDATKEPLQQEDPQEESHLTGAVEHEAARLAWLDAETSKRLKELEELKAKEIDSMQKQRLDWLDAETSRRTKELNELKAEEMYRLQQLSVSATHLADKVEEAVLDRLKPLLVKAQRVNSTTEANIHLKDGSSVNTAKAQPAQEVAAVDFESNNIRQLDDFLEDCASELWAVTHAKILGSETLATVEDSKDSPDLEIMMRRMEEMEKYQESVRQRYNKIAYADPRLWMQEENNDQKISAISEKPLSPHPIRITKTVDRKDPAVNIMLERPCNGNSLDESVGTEEGSEKREAPLLSLAEDSQQKEGRAPLFVPPGMQHSIGDYCSRFEQYLRIISHEAVGSFNPWLIAESFSEELVDEALGAVAAELQDMCEDYAEAVFTSEFLEAAT | |||||||
Modified residue (large scale data) | 93 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 190 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 193 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 287 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 287 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 409 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 564 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 568 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 670 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 672 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 674 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 700 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 700 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 772 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 826 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 826 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Interaction
Subunit
Interacts with CEP63 (PubMed:24613305).
Interacts with WDR62 (PubMed:26297806).
Forms a complex with OFD1 and CEP20/FOR20 (PubMed:26643951).
Interacts with PCM1 (PubMed:26297806, PubMed:26643951).
Interacts with WDR62 (PubMed:26297806).
Forms a complex with OFD1 and CEP20/FOR20 (PubMed:26643951).
Interacts with PCM1 (PubMed:26297806, PubMed:26643951).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 178-192 | Polar residues | ||||
Sequence: SHPGQSDLTVPNSPP | ||||||
Region | 178-201 | Disordered | ||||
Sequence: SHPGQSDLTVPNSPPTHDPGLQPH | ||||||
Region | 401-431 | Disordered | ||||
Sequence: ALERWPSTSPKGERRPLTAKDTFPQETSRPS | ||||||
Region | 490-601 | Disordered | ||||
Sequence: KAGKKKPVTENVPFRKKDTLAPARQQGLRKAERGRQSQPHSKSRVQQTTVSSRLKMNRQPVKDRKAPWIPPNPTSPPASPKCAAWLKVKTSPRDATKEPLQQEDPQEESHLT | ||||||
Compositional bias | 529-545 | Polar residues | ||||
Sequence: HSKSRVQQTTVSSRLKM | ||||||
Compositional bias | 580-601 | Basic and acidic residues | ||||
Sequence: SPRDATKEPLQQEDPQEESHLT | ||||||
Coiled coil | 616-642 | |||||
Sequence: AETSKRLKELEELKAKEIDSMQKQRLD | ||||||
Region | 849-872 | Disordered | ||||
Sequence: RPCNGNSLDESVGTEEGSEKREAP | ||||||
Region | 885-967 | Necessary and sufficient for CEP20-binding | ||||
Sequence: GRAPLFVPPGMQHSIGDYCSRFEQYLRIISHEAVGSFNPWLIAESFSEELVDEALGAVAAELQDMCEDYAEAVFTSEFLEAAT |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q2KHM9-1
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
- Length967
- Mass (Da)109,407
- Last updated2010-05-18 v3
- Checksum2245C5246165B8AA
Q2KHM9-2
- Name2
- Differences from canonical
- 1-299: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_023539 | 1-299 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 178-192 | Polar residues | ||||
Sequence: SHPGQSDLTVPNSPP | ||||||
Sequence conflict | 250 | in Ref. 3; BAF85565 | ||||
Sequence: E → K | ||||||
Compositional bias | 529-545 | Polar residues | ||||
Sequence: HSKSRVQQTTVSSRLKM | ||||||
Compositional bias | 580-601 | Basic and acidic residues | ||||
Sequence: SPRDATKEPLQQEDPQEESHLT | ||||||
Sequence conflict | 821 | in Ref. 1; BAA34473 | ||||
Sequence: S → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB018296 EMBL· GenBank· DDBJ | BAA34473.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK292876 EMBL· GenBank· DDBJ | BAF85565.1 EMBL· GenBank· DDBJ | mRNA | ||
AK296971 EMBL· GenBank· DDBJ | BAH12465.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004706 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC015916 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC113016 EMBL· GenBank· DDBJ | AAI13017.1 EMBL· GenBank· DDBJ | mRNA | ||
BC113017 EMBL· GenBank· DDBJ | AAI13018.1 EMBL· GenBank· DDBJ | mRNA | ||
AL080108 EMBL· GenBank· DDBJ | CAB45712.1 EMBL· GenBank· DDBJ | mRNA |