Q5TZA2 · CROCC_HUMAN

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

Function

function

Major structural component of the ciliary rootlet, a cytoskeletal-like structure in ciliated cells which originates from the basal body at the proximal end of a cilium and extends proximally toward the cell nucleus (By similarity).
Furthermore, is required for the correct positioning of the cilium basal body relative to the cell nucleus, to allow for ciliogenesis (PubMed:27623382).
Contributes to centrosome cohesion before mitosis (PubMed:16203858).

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 Component9+2 motile cilium
Cellular Componentactin cytoskeleton
Cellular Componentcentriole
Cellular Componentcentrosome
Cellular Componentciliary rootlet
Cellular Componentcytosol
Cellular Componentextracellular exosome
Cellular Componentphotoreceptor inner segment
Cellular Componentplasma membrane
Cellular Componentsubapical part of cell
Molecular Functionactin binding
Molecular Functionkinesin binding
Molecular Functionstructural constituent of cytoskeleton
Molecular Functionstructural molecule activity
Biological Processcellular homeostasis
Biological Processcentriole-centriole cohesion
Biological Processcentrosome cycle
Biological Processciliary basal body organization
Biological Processepithelial structure maintenance
Biological Processestablishment of localization in cell
Biological Processestablishment of organelle localization
Biological Processphotoreceptor cell maintenance
Biological Processpositive regulation of cilium assembly
Biological Processpositive regulation of protein localization to cilium
Biological Processprotein localization
Biological Processprotein localization to organelle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Rootletin
  • Alternative names
    • Ciliary rootlet coiled-coil protein

Gene names

    • Name
      CROCC
    • Synonyms
      KIAA0445

Organism names

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

Accessions

  • Primary accession
    Q5TZA2
  • Secondary accessions
    • Q2VHY3
    • Q66GT7
    • Q7Z2L4
    • Q7Z5D7

Proteomes

Organism-specific databases

Subcellular Location

Note: In ciliated cells, associated with ciliary rootlets. In non-ciliated cells, localized between, around and at the proximal ends of the centrioles. Dissociates from the centrioles at the onset of mitosis and reassociates with them at anaphase.

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_0616267in dbSNP:rs6586566
Natural variantVAR_061627372in dbSNP:rs57442576
Natural variantVAR_059628439in dbSNP:rs4463721
Natural variantVAR_059629586in dbSNP:rs9435714
Natural variantVAR_0596301097in dbSNP:rs6669627
Natural variantVAR_0834731216in dbSNP:rs749003874
Natural variantVAR_0834741866in dbSNP:rs374780265

Variants

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

The viewer provides 3,011 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_00002399431-2017UniProtRootletin
Modified residue (large scale data)462PRIDEPhosphoserine
Modified residue (large scale data)483PRIDEPhosphoserine
Modified residue (large scale data)488PRIDEPhosphoserine
Modified residue (large scale data)492PRIDEPhosphothreonine
Modified residue (large scale data)494PRIDEPhosphoserine
Modified residue (large scale data)512PRIDEPhosphoserine
Modified residue (large scale data)516PRIDEPhosphoserine
Modified residue (large scale data)1218PRIDEPhosphoserine
Modified residue (large scale data)1451PRIDEPhosphoserine
Modified residue1460UniProtPhosphoserine
Modified residue (large scale data)1460PRIDEPhosphoserine
Modified residue1470UniProtPhosphoserine
Modified residue1476UniProtPhosphoserine
Modified residue1483UniProtPhosphoserine
Modified residue1486UniProtPhosphoserine
Modified residue1490UniProtPhosphoserine
Modified residue (large scale data)1490PRIDEPhosphoserine
Modified residue1496UniProtPhosphoserine
Modified residue1575UniProtPhosphoserine
Modified residue (large scale data)1619PRIDEPhosphoserine
Modified residue1660UniProtPhosphoserine
Modified residue (large scale data)1660PRIDEPhosphoserine
Modified residue (large scale data)1900PRIDEPhosphoserine
Modified residue (large scale data)2005PRIDEPhosphoserine
Modified residue (large scale data)2009PRIDEPhosphoserine

Post-translational modification

Phosphorylated by NEK2 which may regulate its association with centrosomes.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Homomer. Interacts with KLC3, NEK2 and the N-terminus of CEP250. Interacts with CEP44 (PubMed:31974111).
Interacts with CCDC102B (via N-terminus)

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for coiled coil, compositional bias, region.

TypeIDPosition(s)Description
Coiled coil70-262
Coiled coil318-444
Compositional bias464-499Polar residues
Region464-518Disordered
Coiled coil546-1058
Coiled coil1091-1438
Region1184-1226Disordered
Region1443-1575Disordered
Compositional bias1484-1498Pro residues
Coiled coil1505-1704
Compositional bias1506-1531Basic and acidic residues
Compositional bias1540-1571Basic and acidic residues
Region1962-2017Disordered
Compositional bias1963-1987Basic and acidic residues
Compositional bias1991-2006Polar residues

Sequence similarities

Belongs to the rootletin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q5TZA2-1

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
    2,017
  • Mass (Da)
    228,424
  • Last updated
    2022-02-23 v2
  • Checksum
    5A7167A0A906CF03
MSLGLAGAQEVELTLETVIQTLESSVLCQEKGLGARDLAQDAQITSLPALIREIVTRNLSQPESPVLLPATEMASLLSLQEENQLLQQELSRVEDLLAQSRAERDELAIKYNAVSERLEQALRLEPGELETQEPRGLVRQSVELRRQLQEEQASYRRKLQAYQEGQQRQAQLVQRLQGKILQYKKRCSELEQQLLERSGELEQQRLRDTEHSQDLESALIRLEEEQQRSASLAQVNAMLREQLDQAGSANQALSEDIRKVTNDWTRCRKELEHREAAWRREEESFNAYFSNEHSRLLLLWRQVVGFRRLVSEVKMFTERDLLQLGGELARTSRAVQEAGLGLSTGLRLAESRAEAALEKQALLQAQLEEQLRDKVLREKDLAQQQMQSDLDKADLSARVTELGLAVKRLEKQNLEKDQVNKDLTEKLEALESLRLQEQAALETEDGEGLQQTLRDLAQAVLSDSESGVQLSGSERTADASNGSLRGLSGQRTPSPPRRSSPGRGRSPRRGPSPACSDSSTLALIHSALHKRQLQVQDMRGRYEASQDLLGTLRKQLSDSESERRALEEQLQRLRDKTDGAMQAHEDAQREVQRLRSANELLSREKSNLAHSLQVAQQQAEELRQEREKLQAAQEELRRQRDRLEEEQEDAVQDGARVRRELERSHRQLEQLEGKRSVLAKELVEVREALSRATLQRDMLQAEKAEVAEALTKAEAGRVELELSMTKLRAEEASLQDSLSKLSALNESLAQDKLDLNRLVAQLEEEKSALQGRQRQAEQEATVAREEQERLEELRLEQEVARQGLEGSLRVAEQAQEALEQQLPTLRHERSQLQEQLAQLSRQLSGREQELEQARREAQRQVEALERAAREKEALAKEHAGLAVQLVAAEREGRTLSEEATRLRLEKEALEGSLFEVQRQLAQLEARREQLEAEGQALLLAKETLTGELAGLRQQIIATQEKASLDKELMAQKLVQAEREAQASLREQRAAHEEDLQRLQREKEAAWRELEAERAQLQSQLQREQEELLARLEAEKEELSEEIAALQQERDEGLLLAESEKQQALSLKESEKTALSEKLMGTRHSLATISLEMERQKRDAQSRQEQDRSTVNALTSELRDLRAQREEAAAAHAQEVRRLQEQARDLGKQRDSCLREAEELRTQLRLLEDARDGLRRELLEAQRKLRESQEGREVQRQEAGELRRSLGEGAKEREALRRSNEELRSAVKKAESERISLKLANEDKEQKLALLEEARTAVGKEAGELRTGLQEVERSRLEARRELQELRRQMKMLDSENTRLGRELAELQGRLALGERAEKESRRETLGLRQRLLKGEASLEVMRQELQVAQRKLQEQEGEFRTRERRLLGSLEEARGTEKQQLDHARGLELKLEAARAEAAELGLRLSAAEGRAQGLEAELARVEVQRRAAEAQLGGLRSALRRGLGLGRAPSPAPRPVPGSPARDAPAEGSGEGLNSPSTLECSPGSQPPSPGPATSPASPDLDPEAVRGALREFLQELRSAQRERDELRTQTSALNRQLAEMEAERDSATSRARQLQKAVAESEEARRSVDGRLSGVQAELALQEESVRRSERERRATLDQVATLERSLQATESELRASQEKISKMKANETKLEGDKRRLKEVLDASESRTVKLELQRRSLEGELQRSRLGLSDREAQAQALQDRVDSLQRQVADSEVKAGTLQLTVERLNGALAKVEESEGALRDKVRGLTEALAQSSASLNSTRDKNLHLQKALTACEHDRQVLQERLDAARQALSEARKQSSSLGEQVQTLRGEVADLELQRVEAEGQLQQLREVLRQRQEGEAAALNTVQKLQDERRLLQERLGSLQRALAQLEAEKREVERSALRLEKDRVALRRTLDKVEREKLRSHEDTVRLSAEKGRLDRTLTGAELELAEAQRQIQQLEAQVVVLEQSHSPAQLEVDAQQQQLELQQEVERLRSAQAQTERTLEARERAHRQRVRGLEEQVSTLKGQLQQELRRSSAPFSPPSGPPEK

Q5TZA2-2

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
B1AKD8B1AKD8_HUMANCROCC1311
A0A087WU09A0A087WU09_HUMANCROCC204
A0A087WW81A0A087WW81_HUMANCROCC838

Features

Showing features for alternative sequence, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0520691-697in isoform 2
Compositional bias464-499Polar residues
Compositional bias1484-1498Pro residues
Compositional bias1506-1531Basic and acidic residues
Compositional bias1540-1571Basic and acidic residues
Compositional bias1963-1987Basic and acidic residues
Alternative sequenceVSP_0520701984-1990in isoform 2
Compositional bias1991-2006Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ139275
EMBL· GenBank· DDBJ
ABA43896.1
EMBL· GenBank· DDBJ
mRNA
BX284668
EMBL· GenBank· DDBJ
CAH70055.1
EMBL· GenBank· DDBJ
Genomic DNA
AL049569
EMBL· GenBank· DDBJ
CAH70055.1
EMBL· GenBank· DDBJ
Genomic DNA
AL049569
EMBL· GenBank· DDBJ
CAI20363.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284668
EMBL· GenBank· DDBJ
CAI20363.1
EMBL· GenBank· DDBJ
Genomic DNA
AB007914
EMBL· GenBank· DDBJ
BAA32290.2
EMBL· GenBank· DDBJ
mRNA
AF527734
EMBL· GenBank· DDBJ
AAP85633.1
EMBL· GenBank· DDBJ
mRNA
BK005505
EMBL· GenBank· DDBJ
DAA05505.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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