Q9NXG0 · CNTLN_HUMAN
- ProteinCentlein
- GeneCNTLN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1405 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for centrosome cohesion and recruitment of CEP68 to centrosomes.
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 | centriole | |
Cellular Component | centrosome | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | nucleoplasm | |
Cellular Component | sperm head-tail coupling apparatus | |
Molecular Function | protein domain specific binding | |
Molecular Function | protein kinase binding | |
Molecular Function | protein-macromolecule adaptor activity | |
Biological Process | centriole-centriole cohesion | |
Biological Process | protein localization to organelle | |
Biological Process | protein-containing complex assembly | |
Biological Process | regulation of protein localization | |
Biological Process | single fertilization | |
Biological Process | spermatogenesis |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCentlein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NXG0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with gamma-tubulin during interphase and mitosis. Appears to associate with the mother centriole during G1 phase and with daughter centrioles towards G1/S phase (By similarity).
Localizes to the proximal ends of the centrioles (PubMed:24554434).
Levels are high at interphase centrosomes but are reduced on mitotic spindle poles (PubMed:24554434).
Localizes to the proximal ends of the centrioles (PubMed:24554434).
Levels are high at interphase centrosomes but are reduced on mitotic spindle poles (PubMed:24554434).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_056840 | 284 | in dbSNP:rs3808795 | |||
Sequence: T → A | ||||||
Natural variant | VAR_056841 | 291 | in dbSNP:rs3808794 | |||
Sequence: E → D | ||||||
Natural variant | VAR_025608 | 562 | in dbSNP:rs3808782 | |||
Sequence: R → C | ||||||
Natural variant | VAR_025609 | 695 | in dbSNP:rs7035276 | |||
Sequence: T → I | ||||||
Natural variant | VAR_025610 | 1376 | in dbSNP:rs2499057 | |||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 5 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, 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_0000227567 | 2-1405 | UniProt | Centlein | |||
Sequence: AARSPPSPHPSPPARQLGPRSPRVGRGAEVHAMRSEASGFAGAAREVVADESDKIWVGEEGSGGRRGPGGAAPAHAPLLSAPMGSRRLEGISVEEAMVTRTQLLEEELSSLKEELALCQADKEFVWSLWKRLQVTNPDLTQVVSLVVEREKQKSEAKDRKVLEILQVKDAKIQEFEQRESVLKQEINDLVKRKIAVDEENAFLRKEFSDLEKKFKDKSQEIKDTKECVQNKEEQNRLVIKNLEEENKKLSTRCTDLLNDLEKLRKQEAHLRKEKYSTDAKIKTFEDNLIEARKEVEVSQSKYNALSLQLSNKQTELIQKDMDITLVRKELQELQNLYKQNSTHTAQQAELIQQLQVLNMDTQKVLRNQEDVHTAESISYQKLYNELHICFETTKSNEAMLRQSVTNLQDQLLQKEQENAKLKEKLQESQGAPLPLPQESDPDYSAQVPHRPSLSSLETLMVSQKSEIEYLQEKLKIANEKLSENISANKGFSRKSIMTSAEGKHKEPPVKRSRSLSPKSSFTDSEELQKLRKAERKIENLEKALQLKSQENDELRDAHEKRKERLQMLQTNYRAVKEQLKQWEEGSGMTEIRKIKRADPQQLRQEDSDAVWNELAYFKRENQELMIQKMNLEEELDELKVHISIDKAAIQELNRCVAERREEQLFRSGEDDEVKRSTPEKNGKEMLEQTLQKVTELENRLKSFEKRSRKLKEGNKKLMKENDFLKSLLKQQQEDTETREKELEQIIKGSKDVEKENTELQVKISELETEVTSLRRQVAEANALRNENEELINPMEKSHQSADRAKSEMATMKVRSGRYDCKTTMTKVKFKAAKKNCSVGRHHTVLNHSIKVMSNVFENLSKDGWEDVSESSSDSEAQTSQTLGTIIVETSQKISPTEDGKDQKESDPTEDSQTQGKEIVQTYLNIDGKTPKDYFHDKNAKKPTFQKKNCKMQKSSHTAVPTRVNREKYKNITAQKSSSNIILLRERIISLQQQNSVLQNAKKTAELSVKEYKEVNEKLLHQQQVSDQRFQTSRQTIKKLNLDLAGLRKEKEDLLKKLESSSEITSLAEENSQVTFPRIQVTSLSPSRSMDLEMKQLQYKLKNATNELTKQSSNVKTLKFELLAKEEHIKEMHEKISRMERDITMKRHLIEDLKFRQKVNLESNKSFSEMLQNLDKKVKTLTEECSNKKVSIDSLKQRLNVAVKEKSQYEQMYQKSKEELEKKDLKLTLLVSRISETESAMAEIETAASKQLQELALQSEQVLEGAQKTLLLANEKVEEFTTFVKALAKELQNDVHVVRRQIRELKKMKKNRDACKTSTHKAQTLAASILNISRSDLEEILDTEDQVEIEKTKIDAENDKEWMLYIQKLLEGQSLTLSPRLKCNGAIVAHQNLRLPDSSSSASAS | |||||||
Modified residue | 5 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 5 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 12 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 22 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 861 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1085 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1333 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1343 | UniProt | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated directly or indirectly by NEK2.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with CEP250 and CEP68. Interacts with NEK2; the interaction leads to phosphorylation of CNTLN.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9NXG0-2 | LAS2 Q8IYD9 | 3 | EBI-9640137, EBI-749878 | |
BINARY | Q9NXG0-2 | RFK Q969G6 | 3 | EBI-9640137, EBI-716872 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Pro residues | ||||
Sequence: MAARSPPSPHPSPPARQL | ||||||
Region | 1-79 | Disordered | ||||
Sequence: MAARSPPSPHPSPPARQLGPRSPRVGRGAEVHAMRSEASGFAGAAREVVADESDKIWVGEEGSGGRRGPGGAAPAHAPL | ||||||
Coiled coil | 95-126 | |||||
Sequence: EEAMVTRTQLLEEELSSLKEELALCQADKEFV | ||||||
Region | 421-450 | Disordered | ||||
Sequence: KLKEKLQESQGAPLPLPQESDPDYSAQVPH | ||||||
Region | 493-529 | Disordered | ||||
Sequence: SRKSIMTSAEGKHKEPPVKRSRSLSPKSSFTDSEELQ | ||||||
Compositional bias | 499-513 | Basic and acidic residues | ||||
Sequence: TSAEGKHKEPPVKRS | ||||||
Coiled coil | 613-655 | |||||
Sequence: NELAYFKRENQELMIQKMNLEEELDELKVHISIDKAAIQELNR | ||||||
Coiled coil | 681-793 | |||||
Sequence: KNGKEMLEQTLQKVTELENRLKSFEKRSRKLKEGNKKLMKENDFLKSLLKQQQEDTETREKELEQIIKGSKDVEKENTELQVKISELETEVTSLRRQVAEANALRNENEELIN | ||||||
Region | 865-917 | Disordered | ||||
Sequence: WEDVSESSSDSEAQTSQTLGTIIVETSQKISPTEDGKDQKESDPTEDSQTQGK | ||||||
Compositional bias | 871-894 | Polar residues | ||||
Sequence: SSSDSEAQTSQTLGTIIVETSQKI | ||||||
Compositional bias | 895-912 | Basic and acidic residues | ||||
Sequence: SPTEDGKDQKESDPTEDS | ||||||
Coiled coil | 980-1311 | |||||
Sequence: NIILLRERIISLQQQNSVLQNAKKTAELSVKEYKEVNEKLLHQQQVSDQRFQTSRQTIKKLNLDLAGLRKEKEDLLKKLESSSEITSLAEENSQVTFPRIQVTSLSPSRSMDLEMKQLQYKLKNATNELTKQSSNVKTLKFELLAKEEHIKEMHEKISRMERDITMKRHLIEDLKFRQKVNLESNKSFSEMLQNLDKKVKTLTEECSNKKVSIDSLKQRLNVAVKEKSQYEQMYQKSKEELEKKDLKLTLLVSRISETESAMAEIETAASKQLQELALQSEQVLEGAQKTLLLANEKVEEFTTFVKALAKELQNDVHVVRRQIRELKKMKKN |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9NXG0-1
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
- Length1,405
- Mass (Da)161,571
- Last updated2018-09-12 v6
- Checksum6170160F6995E843
Q9NXG0-2
- Name2
- Differences from canonical
- 1374-1405: SLTLSPRLKCNGAIVAHQNLRLPDSSSSASAS → LPFASYLLEAVLEKINEKKKLVEGYFTIMKDIR
Q9NXG0-3
- Name3
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Pro residues | ||||
Sequence: MAARSPPSPHPSPPARQL | ||||||
Alternative sequence | VSP_032864 | 383-391 | in isoform 3 | |||
Sequence: LYNELHICF → VCFYSVIKM | ||||||
Alternative sequence | VSP_032865 | 392-1405 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 499-513 | Basic and acidic residues | ||||
Sequence: TSAEGKHKEPPVKRS | ||||||
Sequence conflict | 700 | in Ref. 1; BAB13850 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 871 | in Ref. 1; BAB13850 | ||||
Sequence: Missing | ||||||
Compositional bias | 871-894 | Polar residues | ||||
Sequence: SSSDSEAQTSQTLGTIIVETSQKI | ||||||
Compositional bias | 895-912 | Basic and acidic residues | ||||
Sequence: SPTEDGKDQKESDPTEDS | ||||||
Sequence conflict | 1004 | in Ref. 1; BAB13850 | ||||
Sequence: T → A | ||||||
Sequence conflict | 1240 | in Ref. 1; BAB13850 | ||||
Sequence: A → V | ||||||
Alternative sequence | VSP_017558 | 1374-1405 | in isoform 2 | |||
Sequence: SLTLSPRLKCNGAIVAHQNLRLPDSSSSASAS → LPFASYLLEAVLEKINEKKKLVEGYFTIMKDIR | ||||||
Sequence conflict | 1388 | in Ref. 1; BAA91052 | ||||
Sequence: V → M |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK000283 EMBL· GenBank· DDBJ | BAA91052.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK021596 EMBL· GenBank· DDBJ | BAB13850.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK098502 EMBL· GenBank· DDBJ | BAC05319.1 EMBL· GenBank· DDBJ | mRNA | ||
AL133214 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL162725 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL354711 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL354738 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL590377 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |