Q14008 · CKAP5_HUMAN

  • Protein
    Cytoskeleton-associated protein 5
  • Gene
    CKAP5
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Acts as a processive microtubule polymerase. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles. In spindle formation protects kinetochore microtubules from depolymerization by KIF2C and has an essential role in centrosomal microtubule assembly independently of KIF2C activity. Contributes to centrosome integrity. Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (PubMed:23532825).
Enhances the strength of NDC80 complex-mediated kinetochore-tip microtubule attachments (PubMed:27156448).

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 Componentcentrosome
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentkinetochore
Cellular Componentmembrane
Cellular Componentnucleolus
Cellular Componentplasma membrane
Cellular Componentprotein-containing complex
Cellular Componentspindle pole
Molecular Functioncadherin binding
Molecular Functionmicrotubule binding
Molecular Functionmicrotubule plus end polymerase
Molecular Functionmicrotubule plus-end binding
Molecular Functionribonucleoprotein complex binding
Biological Processcell division
Biological Processcentrosome cycle
Biological Processcentrosome duplication
Biological Processestablishment or maintenance of microtubule cytoskeleton polarity
Biological Processmicrotubule depolymerization
Biological Processmicrotubule polymerization
Biological Processmitotic spindle organization
Biological Processpositive regulation of microtubule nucleation
Biological ProcessRNA transport
Biological Processspindle organization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytoskeleton-associated protein 5
  • Alternative names
    • Colonic and hepatic tumor overexpressed gene protein (Ch-TOG)

Gene names

    • Name
      CKAP5
    • Synonyms
      KIAA0097

Organism names

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

Accessions

  • Primary accession
    Q14008
  • Secondary accessions
    • Q05D70
    • Q0VAX7
    • Q0VAX8
    • Q14668
    • Q2TA89
    • Q6NSH4

Proteomes

Organism-specific databases

Subcellular Location

Note: Detected on centrosomes and kinetochores during interphase and mitosis independently from TACC3 and clathrin. Located to spindle poles and microtubules during mitosis. In complex with TACC3 localized to microtubule plus-ends in mitosis and interphase. In complex with TACC3 and clathrin localized to inter-microtubule bridges in mitotic spindles. Accumulation sites at microtubule plus ends protruded approximately 100 nm from MAPRE1/EB1 sites in interphase cells.

Keywords

Disease & Variants

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_045627785in dbSNP:rs11038988
Mutagenesis1939Disrupts interaction with TACC3.
Mutagenesis1939Abolishes localization to spindle microtubules, no effect on localization to centrosomes and kinetochores; when associated with A-1942.
Mutagenesis1942Disrupts interaction with TACC3.
Mutagenesis1942Abolishes localization to spindle microtubules, no effect on localization to centrosomes and kinetochores; when associated with A-1939.

Variants

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

The viewer provides 1,599 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, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00000896631-2032UniProtCytoskeleton-associated protein 5
Modified residue48UniProtN6-acetyllysine
Modified residue (large scale data)247PRIDEPhosphoserine
Modified residue (large scale data)569PRIDEPhosphothreonine
Modified residue816UniProtPhosphoserine
Modified residue (large scale data)816PRIDEPhosphoserine
Modified residue (large scale data)832PRIDEPhosphothreonine
Modified residue845UniProtPhosphoserine
Modified residue (large scale data)845PRIDEPhosphoserine
Modified residue (large scale data)1107PRIDEPhosphoserine
Modified residue (large scale data)1149PRIDEPhosphoserine
Modified residue1469UniProtPhosphoserine
Modified residue (large scale data)1469PRIDEPhosphoserine
Modified residue1861UniProtPhosphoserine
Modified residue (large scale data)1861PRIDEPhosphoserine
Modified residue (large scale data)1964PRIDEPhosphoserine
Modified residue (large scale data)1983PRIDEPhosphoserine
Modified residue (large scale data)1995PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Overexpressed in hepatomas and colonic tumors. Also expressed in skeletal muscle, brain, heart, placenta, lung, liver, kidney and pancreas. Expression is elevated in the brain; highly expressed in the Purkinje cell bodies of the cerebellum.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with TACC1 (PubMed:11903063).
Interacts with SLAIN2 and SLAIN1 (PubMed:21646404).
Interacts with HNRNPA2B1 (PubMed:15703215).
Interacts with TACC3 independently of clathrin (PubMed:25596274).
Interacts with TACC3 and clathrin forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges (PubMed:21297582, PubMed:23532825).
Interacts with NDC80; indicative for an association with the NDC80 complex (PubMed:27156448).

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, repeat, compositional bias.

TypeIDPosition(s)Description
Region1-223TOG 1
Repeat159-197HEAT 1
Region268-502TOG 2
Repeat356-394HEAT 2
Repeat434-472HEAT 3
Region516-579Disordered
Region588-817TOG 3
Repeat750-788HEAT 4
Region811-851Disordered
Region853-1081TOG 4
Repeat855-893HEAT 5
Repeat936-974HEAT 6
Repeat1013-1051HEAT 7
Region1077-1160Disordered
Region1193-1428TOG 5
Repeat1284-1322HEAT 8
Repeat1324-1357HEAT 9
Repeat1361-1399HEAT 10
Region1422-1443Disordered
Region1801-1822Disordered
Region1932-1957Interaction with TACC3
Region1949-2032Disordered
Compositional bias1966-1981Polar residues
Compositional bias1982-1997Basic and acidic residues
Compositional bias1998-2017Polar residues

Domain

The TOG (tumor overexpressed gene) domains are arranged in a N-terminal pentameric array with each domain composed of six (for the most part non-canonical) HEAT repeats forming a oblong paddle-like structure. Intra-HEAT loops are positioned along a face of the TOG domain and bind to a single alpha/beta-tubulin heterodimer. The TOG domains in the array seem to be structurally and functionally polarized. Differential functions may range from microtubule (MT) lattice binding and/or free tubulin heterodimer binding to potentiating stable incorporation of tubulin into the MT lattice.

Sequence similarities

Belongs to the TOG/XMAP215 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q14008-1

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
    2,032
  • Mass (Da)
    225,495
  • Last updated
    2008-11-04 v3
  • Checksum
    B2BBFB1CF2ED688B
MGDDSEWLKLPVDQKCEHKLWKARLSGYEEALKIFQKIKDEKSPEWSKFLGLIKKFVTDSNAVVQLKGLEAALVYVENAHVAGKTTGEVVSGVVSKVFNQPKAKAKELGIEICLMYIEIEKGEAVQEELLKGLDNKNPKIIVACIETLRKALSEFGSKIILLKPIIKVLPKLFESREKAVRDEAKLIAVEIYRWIRDALRPPLQNINSVQLKELEEEWVKLPTSAPRPTRFLRSQQELEAKLEQQQSAGGDAEGGGDDGDEVPQIDAYELLEAVEILSKLPKDFYDKIEAKKWQERKEALESVEVLIKNPKLEAGDYADLVKALKKVVGKDTNVMLVALAAKCLTGLAVGLRKKFGQYAGHVVPTILEKFKEKKPQVVQALQEAIDAIFLTTTLQNISEDVLAVMDNKNPTIKQQTSLFIARSFRHCTASTLPKSLLKPFCAALLKHINDSAPEVRDAAFEALGTALKVVGEKAVNPFLADVDKLKLDKIKECSEKVELIHGKKAGLAADKKEFKPLPGRTAASGAAGDKDTKDISAPKPGPLKKAPAAKAGGPPKKGKPAAPGGAGNTGTKNKKGLETKEIVEPELSIEVCEEKASAVLPPTCIQLLDSSNWKERLACMEEFQKAVELMDRTEMPCQALVRMLAKKPGWKETNFQVMQMKLHIVALIAQKGNFSKTSAQVVLDGLVDKIGDVKCGNNAKEAMTAIAEACMLPWTAEQVVSMAFSQKNPKNQSETLNWLSNAIKEFGFSGLNVKAFISNVKTALAATNPAVRTAAITLLGVMYLYVGPSLRMFFEDEKPALLSQIDAEFEKMQGQSPPAPTRGISKHSTSGTDEGEDGDEPDDGSNDVVDLLPRTEISDKITSELVSKIGDKNWKIRKEGLDEVAGIINDAKFIQPNIGELPTALKGRLNDSNKILVQQTLNILQQLAVAMGPNIKQHVKNLGIPIITVLGDSKNNVRAAALATVNAWAEQTGMKEWLEGEDLSEELKKENPFLRQELLGWLAEKLPTLRSTPTDLILCVPHLYSCLEDRNGDVRKKAQDALPFFMMHLGYEKMAKATGKLKPTSKDQVLAMLEKAKVNMPAKPAPPTKATSKPMGGSAPAKFQPASAPAEDCISSSTEPKPDPKKAKAPGLSSKAKSAQGKKMPSKTSLKEDEDKSGPIFIVVPNGKEQRMKDEKGLKVLKWNFTTPRDEYIEQLKTQMSSCVAKWLQDEMFHSDFQHHNKALAVMVDHLESEKEGVIGCLDLILKWLTLRFFDTNTSVLMKALEYLKLLFTLLSEEEYHLTENEASSFIPYLVVKVGEPKDVIRKDVRAILNRMCLVYPASKMFPFIMEGTKSKNSKQRAECLEELGCLVESYGMNVCQPTPGKALKEIAVHIGDRDNAVRNAALNTIVTVYNVHGDQVFKLIGNLSEKDMSMLEERIKRSAKRPSAAPIKQVEEKPQRAQNISSNANMLRKGPAEDMSSKLNQARSMSGHPEAAQMVRREFQLDLDEIENDNGTVRCEMPELVQHKLDDIFEPVLIPEPKIRAVSPHFDDMHSNTASTINFIISQVASGDINTSIQALTQIDEVLRQEDKAEAMSGHIDQFLIATFMQLRLIYNTHMADEKLEKDEIIKLYSCIIGNMISLFQIESLAREASTGVLKDLMHGLITLMLDSRIEDLEEGQQVIRSVNLLVVKVLEKSDQTNILSALLVLLQDSLLATASSPKFSELVMKCLWRMVRLLPDTINSINLDRILLDIHIFMKVFPKEKLKQCKSEFPIRTLKTLLHTLCKLKGPKILDHLTMIDNKNESELEAHLCRMMKHSMDQTGSKSDKETEKGASRIDEKSSKAKVNDFLAEIFKKIGSKENTKEGLAELYEYKKKYSDADIEPFLKNSSQFFQSYVERGLRVIEMEREGKGRISTSTGISPQMEVTCVPTPTSTVSSIGNTNGEEVGPSVYLERLKILRQRCGLDNTKQDDRPPLTSLLSKPAVPTVASSTDMLHSKLSQLRESREQHQHSDLDSNQTHSSGTVTSSSSTANIDDLKKRLERIKSSRK

Q14008-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q14008-3

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

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H0YDX5H0YDX5_HUMANCKAP5203
H0YEK7H0YEK7_HUMANCKAP5190
H0YCF6H0YCF6_HUMANCKAP5166
E9PQH5E9PQH5_HUMANCKAP5151

Sequence caution

The sequence AAH17856.1 differs from that shown. Reason: Miscellaneous discrepancy Contaminating sequence. Potential poly-A sequence.
The sequence AAH70136.1 differs from that shown. Reason: Miscellaneous discrepancy Contaminating sequence. Potential poly-A sequence.
The sequence AAI11044.1 differs from that shown. Reason: Miscellaneous discrepancy Contaminating sequence. Potential poly-A sequence.
The sequence AAI20871.1 differs from that shown. Reason: Frameshift
The sequence BAA07892.2 differs from that shown. Reason: Erroneous initiation

Features

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

TypeIDPosition(s)Description
Sequence conflict476in Ref. 1; CAA63212 and 2; BAA07892
Alternative sequenceVSP_0356681564-1623in isoform 2
Alternative sequenceVSP_0364001774in isoform 3
Sequence conflict1814in Ref. 1; CAA63212
Sequence conflict1822in Ref. 1; CAA63212
Compositional bias1966-1981Polar residues
Compositional bias1982-1997Basic and acidic residues
Compositional bias1998-2017Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X92474
EMBL· GenBank· DDBJ
CAA63212.1
EMBL· GenBank· DDBJ
mRNA
D43948
EMBL· GenBank· DDBJ
BAA07892.2
EMBL· GenBank· DDBJ
mRNA Different initiation
AC115088
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC017856
EMBL· GenBank· DDBJ
AAH17856.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
BC070136
EMBL· GenBank· DDBJ
AAH70136.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
BC111043
EMBL· GenBank· DDBJ
AAI11044.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
BC120869
EMBL· GenBank· DDBJ
AAI20870.1
EMBL· GenBank· DDBJ
mRNA
BC120870
EMBL· GenBank· DDBJ
AAI20871.1
EMBL· GenBank· DDBJ
mRNA Frameshift

Genome annotation databases

Similar Proteins

Disclaimer

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