Q68D86 · C102B_HUMAN

  • Protein
    Coiled-coil domain-containing protein 102B
  • Gene
    CCDC102B
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

During interphase, forms fibers at the proximal ends of centrioles to maintain centrosome cohesion (PubMed:30404835).
During mitosis, dissociates from the centrosome following phosphorylation to allow centrosome separation (PubMed:30404835).
Contributes to CROCC/rootletin filament formation (PubMed:30404835).

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 Componentcytoplasm
Molecular Functionprotein serine/threonine kinase binding
Biological Processcentriole-centriole cohesion

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Coiled-coil domain-containing protein 102B

Gene names

    • Name
      CCDC102B
    • Synonyms
      C18orf14

Organism names

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

Accessions

  • Primary accession
    Q68D86
  • Secondary accessions
    • A1A4H1
    • Q7Z467
    • Q8NDK7
    • Q9H5C1

Proteomes

Organism-specific databases

Subcellular Location

Note: Concentrated at the proximal ends of centrioles where it forms fibers (PubMed:30404835).
Centrosomal localization becomes weak when cells enter prophase and is significantly decreased in metaphase (PubMed:30404835).

Keywords

Disease & Variants

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis21Substantial decrease in phosphorylation; when associated with A-22, A-34, A-135, A-142, A-194, A-210, A-401, A-404 and A-406.
Mutagenesis22Substantial decrease in phosphorylation; when associated with A-21, A-34, A-135, A-142, A-194, A-210, A-401, A-404 and A-406.
Mutagenesis34Substantial decrease in phosphorylation; when associated with A-21, A-22, A-135, A-142, A-194, A-210, A-401, A-404 and A-406.
Mutagenesis135Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-142, A-194, A-210, A-401, A-404 and A-406.
Mutagenesis142Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-194, A-210, A-401, A-404 and A-406.
Natural variantVAR_047331153in dbSNP:rs572020
Mutagenesis194Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-210, A-401, A-404 and A-406.
Mutagenesis210Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-194, A-401, A-404 and A-406.
Natural variantVAR_047332298in dbSNP:rs2187094
Natural variantVAR_022893346in dbSNP:rs745894
Natural variantVAR_047333370in dbSNP:rs34102373
Mutagenesis401Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-194, A-210, A-404 and A-406.
Mutagenesis404Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-194, A-210, A-401 and A-406.
Mutagenesis406Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-194, A-210, A-401 and A-404.
Natural variantVAR_047334425in dbSNP:rs17080065
Natural variantVAR_022894429in dbSNP:rs9963788

Variants

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

The viewer provides 670 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.

TypeIDPosition(s)Description
ChainPRO_00000793081-513Coiled-coil domain-containing protein 102B
Modified residue21Phosphoserine
Modified residue22Phosphoserine
Modified residue34Phosphoserine
Modified residue135Phosphoserine
Modified residue142Phosphoserine
Modified residue194Phosphoserine
Modified residue210Phosphoserine
Modified residue401Phosphoserine
Modified residue404Phosphoserine
Modified residue406Phosphoserine

Post-translational modification

Phosphorylated directly or indirectly by NEK2 during mitosis which causes dissociation of CCDC102B from the centrosome and allows for centrosome separation.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts (via N-terminus) with centriolar protein CEP250/CNAP1; the interaction results in recruitment of CCDC102B to the proximal ends of centrioles (PubMed:30404835).
Interacts (via N-terminus) with CROCC/rootletin and LRRC45 (PubMed:30404835).
Interacts (via N-terminus) with serine/threonine-protein kinase NEK2; the interaction results in phosphorylation of CCDC102B (PubMed:30404835).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q68D86ABI2 Q9NYB95EBI-10171570, EBI-743598
BINARY Q68D86ABI2 Q9NYB9-23EBI-10171570, EBI-11096309
BINARY Q68D86AK8 Q96MA63EBI-10171570, EBI-8466265
BINARY Q68D86ANKRD23 Q86SG23EBI-10171570, EBI-5661893
BINARY Q68D86ARL4A P406173EBI-10171570, EBI-2875746
BINARY Q68D86ARL4D P497034EBI-10171570, EBI-711726
BINARY Q68D86BYSL Q138956EBI-10171570, EBI-358049
BINARY Q68D86C20orf202 A1L1683EBI-10171570, EBI-18396958
BINARY Q68D86CACNB4 O003053EBI-10171570, EBI-714838
BINARY Q68D86CAPN3 P20807-43EBI-10171570, EBI-11532021
BINARY Q68D86CCDC120 Q96HB53EBI-10171570, EBI-744556
BINARY Q68D86CCDC120 Q96HB5-44EBI-10171570, EBI-10185348
BINARY Q68D86CCHCR1 Q8TD31-36EBI-10171570, EBI-10175300
BINARY Q68D86CDK18 Q070023EBI-10171570, EBI-746238
BINARY Q68D86CEP19 Q96LK06EBI-10171570, EBI-741885
BINARY Q68D86CEP57L1 Q8IYX8-23EBI-10171570, EBI-10181988
BINARY Q68D86CWF19L2 Q2TBE03EBI-10171570, EBI-5453285
BINARY Q68D86DISC1 Q9NRI5-23EBI-10171570, EBI-11988027
BINARY Q68D86DOCK10 Q96BY63EBI-10171570, EBI-748520
BINARY Q68D86EFHC2 Q5JST63EBI-10171570, EBI-2349927
BINARY Q68D86EHHADH Q084264EBI-10171570, EBI-2339219
BINARY Q68D86ENKD1 Q9H0I26EBI-10171570, EBI-744099
BINARY Q68D86EXOC5 O004713EBI-10171570, EBI-949824
BINARY Q68D86FAM161A Q3B8206EBI-10171570, EBI-719941
BINARY Q68D86FAM217B Q9NTX93EBI-10171570, EBI-19153639
BINARY Q68D86FBF1 Q8TES7-63EBI-10171570, EBI-10244131
BINARY Q68D86FH P079543EBI-10171570, EBI-1050358
BINARY Q68D86FLOT1 O759553EBI-10171570, EBI-603643
BINARY Q68D86FNDC11 Q9BVV23EBI-10171570, EBI-744935
BINARY Q68D86GEM P550403EBI-10171570, EBI-744104
BINARY Q68D86GOPC Q9HD263EBI-10171570, EBI-349832
BINARY Q68D86GOPC Q9HD26-24EBI-10171570, EBI-11102276
BINARY Q68D86HMG20B Q9P0W26EBI-10171570, EBI-713401
BINARY Q68D86IKZF3 Q9UKT93EBI-10171570, EBI-747204
BINARY Q68D86KIFC3 Q9BVG83EBI-10171570, EBI-2125614
BINARY Q68D86KPNA3 O005053EBI-10171570, EBI-358297
BINARY Q68D86KRT75 O956783EBI-10171570, EBI-2949715
BINARY Q68D86KRTAP13-3 Q3SY463EBI-10171570, EBI-10241252
BINARY Q68D86LENG1 Q96BZ83EBI-10171570, EBI-726510
BINARY Q68D86LMO4 P619686EBI-10171570, EBI-2798728
BINARY Q68D86LNX1 Q8TBB14EBI-10171570, EBI-739832
BINARY Q68D86LZTS1 Q9Y2503EBI-10171570, EBI-1216080
BINARY Q68D86MAB21L2 Q9Y5863EBI-10171570, EBI-6659161
BINARY Q68D86MAGOHB Q96A726EBI-10171570, EBI-746778
BINARY Q68D86MCM7 P339933EBI-10171570, EBI-355924
BINARY Q68D86MEOX1 P502213EBI-10171570, EBI-2864512
BINARY Q68D86MEOX2 Q6FHY53EBI-10171570, EBI-16439278
BINARY Q68D86MFAP1 P550813EBI-10171570, EBI-1048159
BINARY Q68D86MGC50722 Q8IVT43EBI-10171570, EBI-14086479
BINARY Q68D86MOS P005403EBI-10171570, EBI-1757866
BINARY Q68D86MSX2 P355483EBI-10171570, EBI-6447480
BINARY Q68D86NIF3L1 Q9GZT86EBI-10171570, EBI-740897
BINARY Q68D86NME4 O007463EBI-10171570, EBI-744871
BINARY Q68D86NTAQ1 Q96HA84EBI-10171570, EBI-741158
BINARY Q68D86NXT2 Q9NPJ83EBI-10171570, EBI-752122
BINARY Q68D86PFKFB4 Q168773EBI-10171570, EBI-764534
BINARY Q68D86PHAF1 Q9BSU15EBI-10171570, EBI-946080
BINARY Q68D86PICK1 Q9NRD53EBI-10171570, EBI-79165
BINARY Q68D86PNMA5 Q96PV48EBI-10171570, EBI-10171633
BINARY Q68D86POMC P011893EBI-10171570, EBI-12219503
BINARY Q68D86POP5 Q969H66EBI-10171570, EBI-366525
BINARY Q68D86PPP1R13B Q96KQ43EBI-10171570, EBI-1105153
BINARY Q68D86PPP1R18 Q6NYC86EBI-10171570, EBI-2557469
BINARY Q68D86PRPF18 Q996333EBI-10171570, EBI-2798416
BINARY Q68D86PSMA1 P257866EBI-10171570, EBI-359352
BINARY Q68D86RASAL3 Q86YV03EBI-10171570, EBI-3437896
BINARY Q68D86RCOR3 Q9P2K33EBI-10171570, EBI-743428
BINARY Q68D86RSPH14 Q9UHP66EBI-10171570, EBI-748350
BINARY Q68D86RTL8A Q9BWD33EBI-10171570, EBI-741643
BINARY Q68D86RTL8B Q17RB03EBI-10171570, EBI-10238588
BINARY Q68D86RTL8C A6ZKI33EBI-10171570, EBI-10174072
BINARY Q68D86SDCBP O005603EBI-10171570, EBI-727004
BINARY Q68D86SFN P319473EBI-10171570, EBI-476295
BINARY Q68D86SGF29 Q96ES73EBI-10171570, EBI-743117
BINARY Q68D86SH3RF2 Q8TEC53EBI-10171570, EBI-2130111
BINARY Q68D86SLIRP Q9GZT33EBI-10171570, EBI-1050793
BINARY Q68D86SMARCD1 Q96GM53EBI-10171570, EBI-358489
BINARY Q68D86SNAPIN O952953EBI-10171570, EBI-296723
BINARY Q68D86SORBS3 O605043EBI-10171570, EBI-741237
BINARY Q68D86SPATA18 Q8TC713EBI-10171570, EBI-11334239
BINARY Q68D86SPATA2 Q9UM823EBI-10171570, EBI-744066
BINARY Q68D86SPG21 Q9NZD86EBI-10171570, EBI-742688
BINARY Q68D86SYCE1 Q8N0S23EBI-10171570, EBI-6872807
BINARY Q68D86SYT17 Q9BSW73EBI-10171570, EBI-745392
BINARY Q68D86TCEANC Q8N8B7-23EBI-10171570, EBI-11955057
BINARY Q68D86TCP10L Q8TDR43EBI-10171570, EBI-3923210
BINARY Q68D86TFIP11 Q9UBB93EBI-10171570, EBI-1105213
BINARY Q68D86TNNI1 P192373EBI-10171570, EBI-746692
BINARY Q68D86TPM3 Q5VU623EBI-10171570, EBI-10184033
BINARY Q68D86TRIM27 P143736EBI-10171570, EBI-719493
BINARY Q68D86TRIM54 Q9BYV26EBI-10171570, EBI-2130429
BINARY Q68D86TSGA10IP Q3SY003EBI-10171570, EBI-10241197
BINARY Q68D86TTC23 Q5W5X9-33EBI-10171570, EBI-9090990
BINARY Q68D86VPS52 Q8N1B43EBI-10171570, EBI-2799833
BINARY Q68D86ZBTB32 A0A0C4DGF13EBI-10171570, EBI-10188476
BINARY Q68D86ZBTB42 B2RXF53EBI-10171570, EBI-12287587
BINARY Q68D86ZC2HC1C Q53FD0-26EBI-10171570, EBI-14104088
BINARY Q68D86ZNF20 P170246EBI-10171570, EBI-717634
BINARY Q68D86ZNF250 P15622-33EBI-10171570, EBI-10177272
BINARY Q68D86ZNF572 Q7Z3I76EBI-10171570, EBI-10172590
BINARY Q68D86ZNF620 Q6ZNG03EBI-10171570, EBI-4395669
BINARY Q68D86ZNF688 P0C7X23EBI-10171570, EBI-4395732
BINARY Q68D86ZNF774 Q6NX453EBI-10171570, EBI-10251462

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, coiled coil.

TypeIDPosition(s)Description
Region1-217Required for centriolar localization and for interaction with CEP250, CROCC, LRRC45 and NEK2
Coiled coil72-142
Coiled coil268-337
Coiled coil363-513
Region493-513Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q68D86-1

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
    513
  • Mass (Da)
    60,448
  • Last updated
    2008-11-25 v4
  • Checksum
    450D36A80D6D88C8
MNLDSIHRLIEETQIFQMQQSSIKSRGDMVAPASPPRDTCNTCFPLHGLQSHAAHNFCAHSYNTNKWDICEELRLRELEEVKARAAQMEKTMRWWSDCTANWREKWSKVRAERNSAREEGRQLRIKLEMAMKELSTLKKKQSLPPQKEALEAKVTQDLKLPGFVEESCEHTDQFQLSSQMHESIREYLVKRQFSTKEDTNNKEQGVVIDSLKLSEEMKPNLDGVDLFNNGGSGNGETKTGLRLKAINLPLENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILLGQHNDEMQELSGNIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSPDFKMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQNW

Q68D86-2

  • Name
    2
  • 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
J3KRG3J3KRG3_HUMANCCDC102B92
J3KRT2J3KRT2_HUMANCCDC102B137
J3QL62J3QL62_HUMANCCDC102B124
J3QLG6J3QLG6_HUMANCCDC102B325

Sequence caution

The sequence AAH56269.1 differs from that shown. Reason: Miscellaneous discrepancy wrong intron-exon boundaries.
The sequence AAI26449.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence AAI26451.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAB15706.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence CAD38721.2 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence CAD38721.2 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict131in Ref. 1; CAH18334
Sequence conflict382in Ref. 1; CAH18334
Sequence conflict469in Ref. 1; CAH18334
Alternative sequenceVSP_014688479-483in isoform 2
Alternative sequenceVSP_014689484-513in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CR749520
EMBL· GenBank· DDBJ
CAH18334.2
EMBL· GenBank· DDBJ
mRNA
AL833863
EMBL· GenBank· DDBJ
CAD38721.2
EMBL· GenBank· DDBJ
mRNA Sequence problems.
AC022035
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC096708
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC011087
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC056269
EMBL· GenBank· DDBJ
AAH56269.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
BC126448
EMBL· GenBank· DDBJ
AAI26449.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC126450
EMBL· GenBank· DDBJ
AAI26451.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK027247
EMBL· GenBank· DDBJ
BAB15706.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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