Q8N137 · CNTRB_HUMAN

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

Function

function

Required for centriole duplication. Inhibition of centriole duplication leading to defects in cytokinesis.

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
Molecular Functionprotein domain specific binding
Biological Processcentriole replication
Biological Processcentrosome separation
Biological Processmitotic cytokinetic process
Biological Processregulation of cilium assembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Centrobin
  • Alternative names
    • Centrosomal BRCA2-interacting protein
    • LYST-interacting protein 8

Gene names

    • Name
      CNTROB
    • Synonyms
      LIP8
    • ORF names
      PP1221

Organism names

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

Accessions

  • Primary accession
    Q8N137
  • Secondary accessions
    • A6NHQ1
    • Q331K3
    • Q69YV7
    • Q8NCB8
    • Q8WXV3

Proteomes

Organism-specific databases

Subcellular Location

Note: Centriole-associated, asymmetrically localizes to the daughter centriole.

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_050877439in dbSNP:rs35421969
Natural variantVAR_024787578in dbSNP:rs11650083

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,089 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 chain, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00000762401-903UniProtCentrobin
Modified residue (large scale data)61PRIDEPhosphothreonine
Modified residue (large scale data)62PRIDEPhosphoserine
Modified residue (large scale data)76PRIDEPhosphoserine
Modified residue (large scale data)78PRIDEPhosphoserine
Modified residue80UniProtPhosphoserine
Modified residue (large scale data)80PRIDEPhosphoserine
Modified residue (large scale data)128PRIDEPhosphoserine
Modified residue (large scale data)135PRIDEPhosphoserine
Modified residue (large scale data)743PRIDEPhosphoserine
Modified residue (large scale data)784PRIDEPhosphoserine
Modified residue (large scale data)787PRIDEPhosphoserine
Modified residue (large scale data)788PRIDEPhosphoserine
Modified residue790UniProtPhosphoserine
Modified residue (large scale data)790PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed (at protein level). Highly expressed in testis. Also expressed in spleen, thymus, prostate, small intestine, colon and peripheral blood leukocytes.

Developmental stage

Preferentially incorporated into the newly assembled daughter centriole during centriole assembly at the late G1 or early S phase. Remains in the daughter centrioles throughout the cell cycle. At the next cycle of centriole duplication, its amount on the original daughter centriole eventually decreases.

Gene expression databases

Organism-specific databases

Structure

Family & Domains

Features

Showing features for region, coiled coil, compositional bias.

TypeIDPosition(s)Description
Region1-34Disordered
Region110-140Disordered
Coiled coil196-560
Region365-903Required for centrosome localization
Region471-493Disordered
Compositional bias474-488Basic and acidic residues
Region568-597Disordered
Compositional bias571-588Pro residues
Region669-704Disordered
Compositional bias675-693Basic and acidic residues
Region772-799Disordered
Compositional bias774-789Polar residues
Compositional bias837-859Basic and acidic residues
Region837-903Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (5)
  • Sequence status
    Complete

This entry describes 5 isoforms produced by Alternative splicing.

Q8N137-1

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.

  • Name
    1
  • Synonyms
    Alpha
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    903
  • Mass (Da)
    101,253
  • Last updated
    2002-10-01 v1
  • Checksum
    3F8E6DE4CEF51851
MATSADSPSSPLGAEDLLSDSSEPPGLNQVSSEVTSQLYASLRLSRQAEATARAQLYLPSTSPPHEGLDGFAQELSRSLSVGLEKNLKKKDGSKHIFEMESVRGQLQTMLQTSRDTAYRDPLIPGAGSERREEDSFDSDSTATLLNTRPLQDLSPSSSAQALEELFPRYTSLRPGPPLNPPDFQGLRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQAHWDEANQLLSTTLPPPNPPAPPAGPSSPGPQEPEKEERRVWTMPPMAVALKPVLQQSREARDELPGAPPVLCSSSSDLSLLLGPSFQSQHSFQPLEPKPDLTSSTAGAFSALGAFHPDHRAERPFPEEDPGPDGEGLLKQGLPPAQLEGLKNFLHQLLETVPQNNENPSVDLLPPKSGPLTVPSWEEAPQVPRIPPPVHKTKVPLAMASSLFRVPEPPSSHSQGSGPSSGSPERGGDGLTFPRQLMEVSQLLRLYQARGWGALPAEDLLLYLKRLEHSGTDGRGDNVPRRNTDSRLGEIPRKEIPSQAVPRRLATAPKTEKPPARKKSGHPAPSSMRSRGGVWR

Q8N137-2

  • Name
    2
  • Synonyms
    Beta
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 838-838: G → GYKPGRKEEGFSGWKLDYGEWSG

Q8N137-3

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

Q8N137-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 526-554: AREQARVCELQSGNQQLEEQRVELVERLQ → LLLDPPAPGLRSPRRRRGGSGLCLPWPWP
    • 555-903: Missing

Q8N137-5

  • Name
    5
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 839-864: TDGRGDNVPRRNTDSRLGEIPRKEIP → YKPGRKEEGFSGWKLDYGEWSGCVLH
    • 865-903: Missing

Computationally mapped potential isoform sequences

There are 7 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
I3L465I3L465_HUMANCNTROB77
I3L3N2I3L3N2_HUMANCNTROB13
I3L1Z8I3L1Z8_HUMANCNTROB198
I3L1A6I3L1A6_HUMANCNTROB242
I3L1B0I3L1B0_HUMANCNTROB199
I3L1E9I3L1E9_HUMANCNTROB26
I3L0P9I3L0P9_HUMANCNTROB187

Sequence caution

The sequence AAG49447.1 differs from that shown. Reason: Erroneous translation Wrong choice of frame.
The sequence AAG49447.1 differs from that shown. Reason: Frameshift
The sequence BAC11241.1 differs from that shown. Reason: Erroneous initiation

Features

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

TypeIDPosition(s)Description
Compositional bias474-488Basic and acidic residues
Alternative sequenceVSP_016836526-554in isoform 4
Alternative sequenceVSP_016837555-903in isoform 4
Compositional bias571-588Pro residues
Sequence conflict582in Ref. 7; AAG49447
Compositional bias675-693Basic and acidic residues
Compositional bias774-789Polar residues
Compositional bias837-859Basic and acidic residues
Alternative sequenceVSP_016838838in isoform 2
Alternative sequenceVSP_016839838in isoform 3
Alternative sequenceVSP_016840839-864in isoform 5
Alternative sequenceVSP_016841865-903in isoform 5

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY160226
EMBL· GenBank· DDBJ
AAO22135.1
EMBL· GenBank· DDBJ
mRNA
AY160227
EMBL· GenBank· DDBJ
AAO22136.1
EMBL· GenBank· DDBJ
mRNA
AF331638
EMBL· GenBank· DDBJ
AAL56068.2
EMBL· GenBank· DDBJ
mRNA
AL137669
EMBL· GenBank· DDBJ
CAH10698.1
EMBL· GenBank· DDBJ
mRNA
AL833907
EMBL· GenBank· DDBJ
CAD38763.1
EMBL· GenBank· DDBJ
mRNA
AC104581
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC014055
EMBL· GenBank· DDBJ
AAH14055.3
EMBL· GenBank· DDBJ
mRNA
BC021134
EMBL· GenBank· DDBJ
AAH21134.1
EMBL· GenBank· DDBJ
mRNA
AK074847
EMBL· GenBank· DDBJ
BAC11241.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AF141344
EMBL· GenBank· DDBJ
AAG49447.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.

Genome annotation databases

Similar Proteins

Disclaimer

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