Q9Y4F5 · C170B_HUMAN

  • Protein
    Centrosomal protein of 170 kDa protein B
  • Gene
    CEP170B
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Plays a role in microtubule organization.

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 Componentcytoplasm
Cellular Componentmicrotubule

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Centrosomal protein of 170 kDa protein B
  • Alternative names
    • Centrosomal protein 170B (Cep170B)

Gene names

    • Name
      CEP170B
    • Synonyms
      FAM68C, KIAA0284

Organism names

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

Accessions

  • Primary accession
    Q9Y4F5
  • Secondary accessions
    • Q2KHR7
    • Q86TI7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

PTM/Processing

Features

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

TypeIDPosition(s)SourceDescription
ChainPRO_00002828891-1589UniProtCentrosomal protein of 170 kDa protein B
Modified residue (large scale data)224PRIDEPhosphoserine
Modified residue (large scale data)225PRIDEPhosphotyrosine
Modified residue (large scale data)337PRIDEPhosphoserine
Modified residue (large scale data)358PRIDEPhosphothreonine
Modified residue360UniProtPhosphoserine
Modified residue (large scale data)360PRIDEPhosphoserine
Modified residue (large scale data)371PRIDEPhosphoserine
Modified residue (large scale data)419PRIDEPhosphoserine
Modified residue421UniProtPhosphoserine
Modified residue (large scale data)421PRIDEPhosphoserine
Modified residue (large scale data)423PRIDEPhosphothreonine
Modified residue (large scale data)425PRIDEPhosphoserine
Modified residue (large scale data)427PRIDEPhosphoserine
Modified residue (large scale data)478PRIDEPhosphoserine
Modified residue480UniProtPhosphoserine
Modified residue (large scale data)485PRIDEPhosphothreonine
Modified residue492UniProtPhosphoserine
Modified residue (large scale data)492PRIDEPhosphoserine
Modified residue (large scale data)511PRIDEPhosphoserine
Modified residue (large scale data)512PRIDEPhosphoserine
Modified residue (large scale data)518PRIDEPhosphoserine
Modified residue (large scale data)531PRIDEPhosphothreonine
Modified residue (large scale data)535PRIDEPhosphothreonine
Modified residue536UniProtPhosphoserine
Modified residue542UniProtPhosphothreonine
Modified residue (large scale data)542PRIDEPhosphothreonine
Modified residue (large scale data)565PRIDEPhosphoserine
Modified residue (large scale data)569PRIDEPhosphothreonine
Modified residue597UniProtPhosphoserine
Modified residue (large scale data)597PRIDEPhosphoserine
Modified residue (large scale data)605PRIDEPhosphoserine
Modified residue619UniProtPhosphoserine
Modified residue (large scale data)619PRIDEPhosphoserine
Modified residue655UniProtPhosphoserine
Modified residue (large scale data)655PRIDEPhosphoserine
Modified residue (large scale data)673PRIDEPhosphoserine
Modified residue (large scale data)706PRIDEPhosphoserine
Modified residue711UniProtPhosphoserine
Modified residue (large scale data)711PRIDEPhosphoserine
Modified residue (large scale data)718PRIDEPhosphoserine
Modified residue721UniProtPhosphoserine
Modified residue (large scale data)721PRIDEPhosphoserine
Modified residue746UniProtPhosphoserine
Modified residue748UniProtPhosphoserine
Modified residue751UniProtPhosphoserine
Modified residue753UniProtPhosphoserine
Modified residue772UniProtPhosphoserine
Modified residue (large scale data)772PRIDEPhosphoserine
Modified residue (large scale data)785PRIDEPhosphoserine
Modified residue829UniProtPhosphoserine
Modified residue (large scale data)829PRIDEPhosphoserine
Modified residue853UniProtPhosphoserine
Modified residue (large scale data)853PRIDEPhosphoserine
Modified residue (large scale data)868PRIDEPhosphoserine
Modified residue (large scale data)887PRIDEPhosphoserine
Modified residue (large scale data)888PRIDEPhosphoserine
Modified residue (large scale data)907PRIDEPhosphoserine
Modified residue (large scale data)951PRIDEPhosphoserine
Modified residue954UniProtPhosphoserine
Modified residue (large scale data)954PRIDEPhosphoserine
Modified residue (large scale data)969PRIDEPhosphoserine
Modified residue972UniProtPhosphoserine
Modified residue (large scale data)972PRIDEPhosphoserine
Modified residue (large scale data)975PRIDEPhosphothreonine
Modified residue986UniProtPhosphoserine
Modified residue (large scale data)986PRIDEPhosphoserine
Modified residue988UniProtPhosphoserine
Modified residue (large scale data)988PRIDEPhosphoserine
Modified residue (large scale data)1040PRIDEPhosphoserine
Modified residue (large scale data)1057PRIDEPhosphoserine
Modified residue (large scale data)1088PRIDEPhosphoserine
Modified residue (large scale data)1114PRIDEPhosphoserine
Modified residue (large scale data)1117PRIDEPhosphothreonine
Modified residue1135UniProtPhosphoserine
Modified residue (large scale data)1135PRIDEPhosphoserine
Modified residue (large scale data)1137PRIDEPhosphothreonine
Modified residue1179UniProtPhosphoserine
Modified residue (large scale data)1179PRIDEPhosphoserine
Modified residue (large scale data)1181PRIDEPhosphothreonine
Modified residue (large scale data)1183PRIDEPhosphothreonine
Modified residue (large scale data)1184PRIDEPhosphoserine
Modified residue (large scale data)1196PRIDEPhosphoserine
Modified residue1199UniProtPhosphoserine
Modified residue (large scale data)1199PRIDEPhosphoserine
Modified residue (large scale data)1261PRIDEPhosphoserine
Modified residue (large scale data)1267PRIDEPhosphoserine
Modified residue (large scale data)1285PRIDEPhosphothreonine
Modified residue1304UniProtPhosphothreonine
Modified residue (large scale data)1304PRIDEPhosphothreonine
Modified residue1356UniProtPhosphoserine
Modified residue1362UniProtPhosphoserine
Modified residue (large scale data)1413PRIDEPhosphoserine
Modified residue1545UniProtPhosphoserine
Modified residue (large scale data)1545PRIDEPhosphoserine
Modified residue1548UniProtPhosphoserine
Modified residue (large scale data)1548PRIDEPhosphoserine
Modified residue (large scale data)1551PRIDEPhosphoserine
Modified residue (large scale data)1569PRIDEPhosphoserine
Modified residue (large scale data)1574PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain23-73FHA
Region130-261Disordered
Region287-309Disordered
Region325-388Disordered
Compositional bias328-362Basic and acidic residues
Region409-583Disordered
Compositional bias428-442Basic and acidic residues
Compositional bias517-550Pro residues
Region598-895Disordered
Compositional bias681-705Basic and acidic residues
Compositional bias763-777Basic and acidic residues
Region934-1316Disordered
Compositional bias954-982Polar residues
Compositional bias1025-1043Basic and acidic residues
Compositional bias1092-1121Polar residues
Compositional bias1126-1140Basic and acidic residues
Compositional bias1220-1261Polar residues
Compositional bias1276-1292Polar residues
Region1350-1374Disordered
Compositional bias1357-1374Polar residues
Region1532-1552Disordered

Sequence similarities

Belongs to the CEP170 family.

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q9Y4F5-1

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
    1,589
  • Mass (Da)
    171,688
  • Last updated
    2007-04-03 v4
  • Checksum
    B232960C12A81244
MSATSWFLVSSSGARHRLPRELIFVGREECELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVLERVQHRVPEEALKHEKYTSQLQVSVKGLAPKRSEALPEHTPYCEASNPRPEKGDRRPGTEAASYRTPLYGQPSWWGEDDGSTLPDAQRQGEPYPERPKGPVQQDGELHGFRAPAEPQGCSFRREPSYFEIPTKETPQPSQPPEVPAHEMPTKDAEAGGGGAAPVVQSHASFTIEFDDCSPGKMKIKDHITKFSLRQRRPPGKEATPGEMVSAETKVADWLVQNDPSLLHRVGPGDDRHSTKSDLPVHTRTLKGHKHEDGTQSDSEDPLAKAASAAGVPLEASGEQVRLQRQIKRDPQELLHNQQAFVIEFFDEDTPRKKRSQSFTHSPSGDPKADKRRGPTPADRDRPSVPAPVQAGGRSSGPQRAGSLKREKTEERLGSPSPASRTPARPFGSVGRRSRLAQDFMAQCLRESSPAARPSPEKVPPVLPAPLTPHGTSPVGPPTPPPAPTDPQLTKARKQEEDDSLSDAGTYTIETEAQDTEVEEARKMIDQVFGVLESPELSRASSATFRPVIRGDRDESDDGGVAQRMALLQEFASRPLGAAPQAEHQGLPVPGSPGGQKWVSRWASLADSYSDPGLTEDGLGRRGGEPEGSLPVRMRRRLPQLPSERADSPAGPESSRRSGPGPPELDSEQPSRLFGQEELDPDSLSDASGSDGGRGPEPGVEPQDSRRRSPQEGPTWSRGRRSPRAPGEPTPASFFIGDQNGDAVLSRKPLAAPGDGEGLGQTAQPSPPARDGVYVSANGRMVIQLRPGRSPEPDGPAPAFLRQESFTKEPASGPPAPGKPPHISSHPLLQDLAATRAARMDFHSQDTHLILKETETALAALEARLLSNSVDAECEGGSTPRPPEDALSGDSDVDTASTVSLRSGKSGPSPTTPQPLRAQKEMSPSPPAAQDPGGTALVSAREQSSERQHHPLGPTDMGRGEPVRRSAIRRGHRPRGSLDWPSEERGPVLAHLPSSDVMASNHETPEATGAGRLGSRRKPAAPPPSPAAREEQSRSSASSQKGPQALTRSNSLSTPRPTRASRLRRARLGDASDTEAADGERGSLGNPEPVGRPAAEQAKKLSRLDILAMPRKRAGSFTGTSDPEAAPARTSFSGRSVELCCASRKPTMAEARAVSRKAANTATTTGPRQPFSRARSGSARYTSNTRRRQQGSDYTSTSEEEYGSRHGSPKHTRSHTSTATQTPRAGSSSRARSRAPGPRDTDDDEEEPDPYGFIVQTAEIAEIARLSQTLVKDVAILAQEIHDVAGDGDTLGSSEPAHSASLSNMPSTPASTISAREELVQRIPEASLNFQKVPPGSLNSRDFDQNMNDSCEDALANKTRPRNREEVIFDNLMLNPVSQLSQAIRENTEHLAEKMKILFQNTGRAWEDLEARINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPSGSLDLLTGNRSLASSAQPGLGKGRVAAQSPPSPASAEALLPALPLRNFPQRASCGPPSLPDPTFLPDAERFLI

Q9Y4F5-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1247-1282: NTRRRQQGSDYTSTSEEEYGSRHGSPKHTRSHTSTA → T

Q9Y4F5-3

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

Sequence caution

The sequence AAH47913.1 differs from that shown. Reason: Frameshift
The sequence BAA22953.3 differs from that shown. Reason: Erroneous initiation

Features

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

TypeIDPosition(s)Description
Alternative sequenceVSP_0242471-70in isoform 3
Sequence conflict315in Ref. 1; BAA22953
Compositional bias328-362Basic and acidic residues
Compositional bias428-442Basic and acidic residues
Compositional bias517-550Pro residues
Compositional bias681-705Basic and acidic residues
Compositional bias763-777Basic and acidic residues
Compositional bias954-982Polar residues
Compositional bias1025-1043Basic and acidic residues
Compositional bias1092-1121Polar residues
Compositional bias1126-1140Basic and acidic residues
Compositional bias1220-1261Polar residues
Alternative sequenceVSP_0242481247-1282in isoform 2
Compositional bias1276-1292Polar residues
Compositional bias1357-1374Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB006622
EMBL· GenBank· DDBJ
BAA22953.3
EMBL· GenBank· DDBJ
mRNA Different initiation
AL583810
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC047913
EMBL· GenBank· DDBJ
AAH47913.1
EMBL· GenBank· DDBJ
mRNA Frameshift
BC112928
EMBL· GenBank· DDBJ
AAI12929.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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