Q9NXG0 · CNTLN_HUMAN

  • Protein
    Centlein
  • Gene
    CNTLN
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Required for centrosome cohesion and recruitment of CEP68 to centrosomes.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcentriole
Cellular Componentcentrosome
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentextracellular exosome
Cellular Componentnucleoplasm
Cellular Componentsperm head-tail coupling apparatus
Molecular Functionprotein domain specific binding
Molecular Functionprotein kinase binding
Molecular Functionprotein-macromolecule adaptor activity
Biological Processcentriole-centriole cohesion
Biological Processprotein localization to organelle
Biological Processprotein-containing complex assembly
Biological Processregulation of protein localization
Biological Processsingle fertilization
Biological Processspermatogenesis

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Centlein
  • Alternative names
    • Centrosomal protein

Gene names

    • Name
      CNTLN
    • Synonyms
      C9orf101, C9orf39

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9NXG0
  • Secondary accessions
    • A5Z2X6
    • Q5VYJ0
    • Q8N1G9
    • Q9HAJ5

Proteomes

Organism-specific databases

Subcellular Location

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).

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_056840284in dbSNP:rs3808795
Natural variantVAR_056841291in dbSNP:rs3808794
Natural variantVAR_025608562in dbSNP:rs3808782
Natural variantVAR_025609695in dbSNP:rs7035276
Natural variantVAR_0256101376in dbSNP:rs2499057

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.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Initiator methionine1UniProtRemoved
Modified residue2UniProtN-acetylalanine
ChainPRO_00002275672-1405UniProtCentlein
Modified residue5UniProtPhosphoserine
Modified residue (large scale data)5PRIDEPhosphoserine
Modified residue (large scale data)8PRIDEPhosphoserine
Modified residue (large scale data)12PRIDEPhosphoserine
Modified residue22UniProtPhosphoserine
Modified residue (large scale data)861PRIDEPhosphoserine
Modified residue (large scale data)1085PRIDEPhosphoserine
Modified residue (large scale data)1333PRIDEPhosphoserine
Modified residue1343UniProtPhosphothreonine

Post-translational modification

Phosphorylated directly or indirectly by NEK2.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with CEP250 and CEP68. Interacts with NEK2; the interaction leads to phosphorylation of CNTLN.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9NXG0-2LAS2 Q8IYD93EBI-9640137, EBI-749878
BINARY Q9NXG0-2RFK Q969G63EBI-9640137, EBI-716872

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for compositional bias, region, coiled coil.

TypeIDPosition(s)Description
Compositional bias1-18Pro residues
Region1-79Disordered
Coiled coil95-126
Region421-450Disordered
Region493-529Disordered
Compositional bias499-513Basic and acidic residues
Coiled coil613-655
Coiled coil681-793
Region865-917Disordered
Compositional bias871-894Polar residues
Compositional bias895-912Basic and acidic residues
Coiled coil980-1311

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

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.

  • Length
    1,405
  • Mass (Da)
    161,571
  • Last updated
    2018-09-12 v6
  • Checksum
    6170160F6995E843
MAARSPPSPHPSPPARQLGPRSPRVGRGAEVHAMRSEASGFAGAAREVVADESDKIWVGEEGSGGRRGPGGAAPAHAPLLSAPMGSRRLEGISVEEAMVTRTQLLEEELSSLKEELALCQADKEFVWSLWKRLQVTNPDLTQVVSLVVEREKQKSEAKDRKVLEILQVKDAKIQEFEQRESVLKQEINDLVKRKIAVDEENAFLRKEFSDLEKKFKDKSQEIKDTKECVQNKEEQNRLVIKNLEEENKKLSTRCTDLLNDLEKLRKQEAHLRKEKYSTDAKIKTFEDNLIEARKEVEVSQSKYNALSLQLSNKQTELIQKDMDITLVRKELQELQNLYKQNSTHTAQQAELIQQLQVLNMDTQKVLRNQEDVHTAESISYQKLYNELHICFETTKSNEAMLRQSVTNLQDQLLQKEQENAKLKEKLQESQGAPLPLPQESDPDYSAQVPHRPSLSSLETLMVSQKSEIEYLQEKLKIANEKLSENISANKGFSRKSIMTSAEGKHKEPPVKRSRSLSPKSSFTDSEELQKLRKAERKIENLEKALQLKSQENDELRDAHEKRKERLQMLQTNYRAVKEQLKQWEEGSGMTEIRKIKRADPQQLRQEDSDAVWNELAYFKRENQELMIQKMNLEEELDELKVHISIDKAAIQELNRCVAERREEQLFRSGEDDEVKRSTPEKNGKEMLEQTLQKVTELENRLKSFEKRSRKLKEGNKKLMKENDFLKSLLKQQQEDTETREKELEQIIKGSKDVEKENTELQVKISELETEVTSLRRQVAEANALRNENEELINPMEKSHQSADRAKSEMATMKVRSGRYDCKTTMTKVKFKAAKKNCSVGRHHTVLNHSIKVMSNVFENLSKDGWEDVSESSSDSEAQTSQTLGTIIVETSQKISPTEDGKDQKESDPTEDSQTQGKEIVQTYLNIDGKTPKDYFHDKNAKKPTFQKKNCKMQKSSHTAVPTRVNREKYKNITAQKSSSNIILLRERIISLQQQNSVLQNAKKTAELSVKEYKEVNEKLLHQQQVSDQRFQTSRQTIKKLNLDLAGLRKEKEDLLKKLESSSEITSLAEENSQVTFPRIQVTSLSPSRSMDLEMKQLQYKLKNATNELTKQSSNVKTLKFELLAKEEHIKEMHEKISRMERDITMKRHLIEDLKFRQKVNLESNKSFSEMLQNLDKKVKTLTEECSNKKVSIDSLKQRLNVAVKEKSQYEQMYQKSKEELEKKDLKLTLLVSRISETESAMAEIETAASKQLQELALQSEQVLEGAQKTLLLANEKVEEFTTFVKALAKELQNDVHVVRRQIRELKKMKKNRDACKTSTHKAQTLAASILNISRSDLEEILDTEDQVEIEKTKIDAENDKEWMLYIQKLLEGQSLTLSPRLKCNGAIVAHQNLRLPDSSSSASAS

Q9NXG0-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1374-1405: SLTLSPRLKCNGAIVAHQNLRLPDSSSSASAS → LPFASYLLEAVLEKINEKKKLVEGYFTIMKDIR

Q9NXG0-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Sequence caution

The sequence BAA91052.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAB13850.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias1-18Pro residues
Alternative sequenceVSP_032864383-391in isoform 3
Alternative sequenceVSP_032865392-1405in isoform 3
Compositional bias499-513Basic and acidic residues
Sequence conflict700in Ref. 1; BAB13850
Sequence conflict871in Ref. 1; BAB13850
Compositional bias871-894Polar residues
Compositional bias895-912Basic and acidic residues
Sequence conflict1004in Ref. 1; BAB13850
Sequence conflict1240in Ref. 1; BAB13850
Alternative sequenceVSP_0175581374-1405in isoform 2
Sequence conflict1388in Ref. 1; BAA91052

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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.

Genome annotation databases

Similar Proteins

Disclaimer

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